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  • Transcription, Genetic
  • American Association for the Advancement of Science (AAAS)  (241)
  • American Chemical Society (ACS)
  • National Academy of Sciences
  • PANGAEA
  • 1995-1999  (90)
  • 1985-1989  (151)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (241)
  • American Chemical Society (ACS)
  • National Academy of Sciences
  • PANGAEA
Years
Year
  • 1
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    Notch signaling: cell fate control and signal integration in development (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-30
    Description: Notch signaling defines an evolutionarily ancient cell interaction mechanism, which plays a fundamental role in metazoan development. Signals exchanged between neighboring cells through the Notch receptor can amplify and consolidate molecular differences, which eventually dictate cell fates. Thus, Notch signals control how cells respond to intrinsic or extrinsic developmental cues that are necessary to unfold specific developmental programs. Notch activity affects the implementation of differentiation, proliferation, and apoptotic programs, providing a general developmental tool to influence organ formation and morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Artavanis-Tsakonas, S -- Rand, M D -- Lake, R J -- NS26084/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Apr 30;284(5415):770-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts General Hospital Cancer Center, Department of Cell Biology, Harvard Medical School, Building 149, 13th Street, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10221902" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Cell Communication ; Cell Division ; Cell Nucleus/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Ligands ; Membrane Proteins/*physiology ; Receptors, Cell Surface/*physiology ; Receptors, Notch ; *Signal Transduction ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Coordinated regulation of iron-controlling genes, H-ferritin and IRP2, by c-MYC (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-01-29
    Description: The protein encoded by the c-MYC proto-oncogene is a transcription factor that can both activate and repress the expression of target genes, but few of its transcriptional targets have been identified. Here, c-MYC is shown to repress the expression of the heavy subunit of the protein ferritin (H-ferritin), which sequesters intracellular iron, and to stimulate the expression of the iron regulatory protein-2 (IRP2), which increases the intracellular iron pool. Down-regulation of the expression of H-ferritin gene was required for cell transformation by c-MYC. These results indicate that c-MYC coordinately regulates genes controlling intracellular iron concentrations and that this function is essential for the control of cell proliferation and transformation by c-MYC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, K J -- Polack, A -- Dalla-Favera, R -- CA-37165/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Jan 29;283(5402):676-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Oncology, Department of Pathology, Columbia University, New York, NY 10032, USA. an.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9924025" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Line ; Cell Line, Transformed ; Cell Transformation, Neoplastic ; DNA/biosynthesis ; Down-Regulation ; Ferritins/*genetics/metabolism ; *Gene Expression Regulation ; Genes, myc ; Homeostasis ; Iron/*metabolism ; Iron Regulatory Protein 2 ; Iron-Regulatory Proteins ; Iron-Sulfur Proteins/*genetics/metabolism ; Proto-Oncogene Proteins c-myc/*physiology ; RNA/metabolism ; RNA-Binding Proteins/*genetics/metabolism ; Receptors, Transferrin/genetics ; Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Role of DNA 5-methylcytosine transferase in cell transformation by fos (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-01-15
    Description: The Fos and Jun oncoproteins form dimeric complexes that stimulate transcription of genes containing activator protein-1 regulatory elements. We found, by representational difference analysis, that expression of DNA 5-methylcytosine transferase (dnmt1) in fos-transformed cells is three times the expression in normal fibroblasts and that fos-transformed cells contain about 20 percent more 5-methylcytosine than normal fibroblasts. Transfection of the gene encoding Dnmt1 induced morphological transformation, whereas inhibition of dnmt1 expression or activity resulted in reversion of fos transformation. Inhibition of histone deacetylase, which associates with methylated DNA, also caused reversion. These results suggest that fos may transform cells through alterations in DNA methylation and in histone deacetylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bakin, A V -- Curran, T -- P30 CA21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Jan 15;283(5400):387-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9888853" target="_blank"〉PubMed〈/a〉
    Keywords: 5-Methylcytosine ; Acetylation ; Animals ; Cell Size ; *Cell Transformation, Neoplastic ; Cytosine/analogs & derivatives/metabolism ; DNA (Cytosine-5-)-Methyltransferase/genetics/*metabolism ; DNA Methylation ; Enzyme Inhibitors/pharmacology ; Gene Expression Regulation, Neoplastic ; *Genes, fos ; Histone Deacetylase Inhibitors ; Histones/metabolism ; Hydroxamic Acids/pharmacology ; Proto-Oncogene Proteins c-fos/*metabolism ; Rats ; Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
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  • 4
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    Apoptosis of T cells mediated by Ca2+-induced release of the transcription factor MEF2 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-10-26
    Description: T cell receptor (TCR)-induced apoptosis of thymocytes is mediated by calcium-dependent expression of the steroid receptors Nur77 and Nor1. Nur77 expression is controlled by the transcription factor myocyte enhancer factor 2 (MEF2), but how MEF2 is activated by calcium signaling is still obscure. Cabin1, a calcineurin inhibitor, was found to regulate MEF2. MEF2 was normally sequestered by Cabin1 in a transcriptionally inactive state. TCR engagement led to an increase in intracellular calcium concentration and the dissociation of MEF2 from Cabin1, as a result of competitive binding of activated calmodulin to Cabin1. The interplay between Cabin1, MEF2, and calmodulin defines a distinct signaling pathway from the TCR to the Nur77 promoter during T cell apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Youn, H D -- Sun, L -- Prywes, R -- Liu, J O -- GM55783/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):790-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research, Department of Biology, Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10531067" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; *Apoptosis ; Calcineurin/chemistry/genetics/metabolism/pharmacology ; Calcium/metabolism ; *Calcium Signaling ; Calmodulin/metabolism ; Cell Line ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Gene Expression ; Genes, Reporter ; Humans ; Jurkat Cells ; MEF2 Transcription Factors ; Myogenic Regulatory Factors ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Phosphoproteins/chemistry/genetics/metabolism/pharmacology ; Receptors, Antigen, T-Cell/metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; T-Lymphocytes/*cytology/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic ; Two-Hybrid System Techniques
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  • 5
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    A species of small antisense RNA in posttranscriptional gene silencing in plants (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-05
    Description: Posttranscriptional gene silencing (PTGS) is a nucleotide sequence-specific defense mechanism that can target both cellular and viral mRNAs. Here, three types of transgene-induced PTGS and one example of virus-induced PTGS were analyzed in plants. In each case, antisense RNA complementary to the targeted mRNA was detected. These RNA molecules were of a uniform length, estimated at 25 nucleotides, and their accumulation required either transgene sense transcription or RNA virus replication. Thus, the 25-nucleotide antisense RNA is likely synthesized from an RNA template and may represent the specificity determinant of PTGS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, A J -- Baulcombe, D C -- New York, N.Y. -- Science. 1999 Oct 29;286(5441):950-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sainsbury Laboratory, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10542148" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/genetics ; *Gene Expression Regulation, Plant ; *Gene Silencing ; Green Fluorescent Proteins ; Luminescent Proteins/genetics ; Plants/enzymology/genetics/virology ; Plants, Genetically Modified ; Plants, Toxic ; Potexvirus/genetics ; RNA, Antisense/analysis/*physiology ; RNA, Messenger/analysis/physiology ; RNA, Plant/analysis/*physiology ; RNA, Viral/metabolism ; Tobacco/genetics ; Transcription, Genetic
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  • 6
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    Genetic selection of peptide inhibitors of biological pathways (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-27
    Description: Genetic selections were used to find peptides that inhibit biological pathways in budding yeast. The peptides were presented inside cells as peptamers, surface loops on a highly expressed and biologically inert carrier protein, a catalytically inactive derivative of staphylococcal nuclease. Peptamers that inhibited the pheromone signaling pathway, transcriptional silencing, and the spindle checkpoint were isolated. Putative targets for the inhibitors were identified by a combination of two-hybrid analysis and genetic dissection of the target pathways. This analysis identified Ydr517w as a component of the spindle checkpoint and reinforced earlier indications that Ste50 has both positive and negative roles in pheromone signaling. Analysis of transcript arrays showed that the peptamers were highly specific in their effects, which suggests that they may be useful reagents in organisms that lack sophisticated genetics as well as for identifying components of existing biological pathways that are potential targets for drug discovery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norman, T C -- Smith, D L -- Sorger, P K -- Drees, B L -- O'Rourke, S M -- Hughes, T R -- Roberts, C J -- Friend, S H -- Fields, S -- Murray, A W -- P41-RR11823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 23;285(5427):591-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, CA 94143-0444, USA. tnorman@microbia.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10417390" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Fungal Proteins/metabolism ; G1 Phase ; Galactose/metabolism ; Lipoproteins/metabolism ; Micrococcal Nuclease ; Mitosis ; Molecular Sequence Data ; Peptide Library ; Peptides/genetics/metabolism/*pharmacology ; Pheromones/*metabolism ; Protein Binding ; Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; *Selection, Genetic ; *Signal Transduction ; Spindle Apparatus/drug effects/*metabolism ; Transcription, Genetic
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  • 7
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    Do proteins predate DNA? (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freeland, S J -- Knight, R D -- Landweber, L F -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):690-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10577226" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; *DNA/biosynthesis/chemistry ; DNA-Directed DNA Polymerase/metabolism ; *Evolution, Molecular ; Genetic Code ; Protein Biosynthesis ; *Proteins/chemistry/metabolism ; *RNA/chemistry/metabolism ; RNA, Catalytic/metabolism ; Ribonucleotide Reductases/metabolism ; Ribonucleotides/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 8
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    Type III secretion machines: bacterial devices for protein delivery into host cells (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-21
    Description: Several Gram-negative pathogenic bacteria have evolved a complex protein secretion system termed type III to deliver bacterial effector proteins into host cells that then modulate host cellular functions. These bacterial devices are present in both plant and animal pathogenic bacteria and are evolutionarily related to the flagellar apparatus. Although type III secretion systems are substantially conserved, the effector molecules they deliver are unique for each bacterial species. Understanding the biology of these devices may allow the development of novel prevention and therapeutic approaches for several infectious diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galan, J E -- Collmer, A -- AI30491/AI/NIAID NIH HHS/ -- GM52543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 21;284(5418):1322-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis, Boyer Center for Molecular Medicine, Yale School of Medicine, New Haven, CT 06536, USA. jorge.galan@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10334981" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Outer Membrane Proteins/genetics/*metabolism/secretion ; Bacterial Proteins/genetics/*metabolism/secretion ; Flagella/metabolism ; Genes, Bacterial ; Gram-Negative Bacteria/genetics/*metabolism/pathogenicity ; Gram-Negative Bacterial Infections/*microbiology ; Humans ; Plants/microbiology ; Protein Biosynthesis ; Transcription, Genetic ; Virulence
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Truncated RanGAP encoded by the Segregation Distorter locus of Drosophila (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-12
    Description: Segregation Distorter (SD) in Drosophila melanogaster is a naturally occurring meiotic drive system in which the SD chromosome is transmitted from SD/SD+ males in vast excess over its homolog owing to the induced dysfunction of SD+-bearing spermatids. The Sd locus is the key distorting gene responsible for this phenotype. A genomic fragment from the Sd region conferred full distorting activity when introduced into the appropriate genetic background by germline transformation. The only functional product encoded by this fragment is a truncated version of the RanGAP nuclear transport protein. These results demonstrate that this mutant RanGAP is the functional Sd product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merrill, C -- Bayraktaroglu, L -- Kusano, A -- Ganetzky, B -- New York, N.Y. -- Science. 1999 Mar 12;283(5408):1742-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, 445 Henry Mall, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10073941" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/chemistry/*genetics/physiology ; Cell Nucleus/metabolism ; Crosses, Genetic ; DNA, Complementary ; *Drosophila Proteins ; Drosophila melanogaster/*genetics/physiology ; Female ; *GTPase-Activating Proteins ; Gene Duplication ; Gene Expression ; *Genes, Insect ; Male ; *Meiosis ; Nuclear Proteins/chemistry/*genetics/physiology ; RNA, Messenger/genetics ; Spermatids/physiology ; Sulfotransferases/chemistry/genetics ; Transcription, Genetic ; Transformation, Genetic
    Print ISSN: 0036-8075
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  • 10
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    UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-21
    Description: Modification of cell surface molecules with sialic acid is crucial for their function in many biological processes, including cell adhesion and signal transduction. Uridine diphosphate-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase) is an enzyme that catalyzes an early, rate-limiting step in the sialic acid biosynthetic pathway. UDP-GlcNAc 2-epimerase was found to be a major determinant of cell surface sialylation in human hematopoietic cell lines and a critical regulator of the function of specific cell surface adhesion molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keppler, O T -- Hinderlich, S -- Langner, J -- Schwartz-Albiez, R -- Reutter, W -- Pawlita, M -- New York, N.Y. -- Science. 1999 May 21;284(5418):1372-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Applied Tumor Virology Program, Tumor Immunology Program, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10334995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; Antigens, CD14/biosynthesis ; Antigens, CD15/biosynthesis ; Antigens, Differentiation, B-Lymphocyte/metabolism ; Carbohydrate Epimerases/genetics/metabolism ; Cell Adhesion Molecules/metabolism ; Cell Membrane/*metabolism ; Culture Media ; *Escherichia coli Proteins ; Glycoconjugates/*metabolism ; HL-60 Cells ; Histocompatibility Antigens Class I/biosynthesis ; Humans ; Lectins/metabolism ; Oligosaccharides/biosynthesis ; Rats ; Sialic Acid Binding Ig-like Lectin 2 ; Sialic Acids/*biosynthesis ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured
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  • 11
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    Exon shuffling by L1 retrotransposition (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-05
    Description: Long interspersed nuclear elements (LINE-1s or L1s) are the most abundant retrotransposons in the human genome, and they serve as major sources of reverse transcriptase activity. Engineered L1s retrotranspose at high frequency in cultured human cells. Here it is shown that L1s insert into transcribed genes and retrotranspose sequences derived from their 3' flanks to new genomic locations. Thus, retrotransposition-competent L1s provide a vehicle to mobilize non-L1 sequences, such as exons or promoters, into existing genes and may represent a general mechanism for the evolution of new genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moran, J V -- DeBerardinis, R J -- Kazazian, H H Jr -- GM45398/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Mar 5;283(5407):1530-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Pennsylvania School of Medicine, Philadelphia, PA, 19104-6145 USA. moranj@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10066175" target="_blank"〉PubMed〈/a〉
    Keywords: Codon, Initiator ; Exons/*genetics ; Expressed Sequence Tags ; Gene Expression ; *Genome, Human ; Gentamicins/pharmacology ; HeLa Cells ; Humans ; Introns ; Long Interspersed Nucleotide Elements/*genetics ; Poly A/metabolism ; Promoter Regions, Genetic ; *Recombination, Genetic ; Transcription, Genetic
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  • 12
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    Roles of phosphorylation sites in regulating activity of the transcription factor Pho4 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-13
    Description: Transcription factors are often phosphorylated at multiple sites. Here it is shown that multiple phosphorylation sites on the budding yeast transcription factor Pho4 play distinct and separable roles in regulating the factor's activity. Phosphorylation of Pho4 at two sites promotes the factor's nuclear export and phosphorylation at a third site inhibits its nuclear import. Phosphorylation of a fourth site blocks the interaction of Pho4 with the transcription factor Pho2. Multiple phosphorylation sites provide overlapping and partially redundant layers of regulation that function to efficiently control the activity of Pho4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Komeili, A -- O'Shea, E K -- New York, N.Y. -- Science. 1999 May 7;284(5416):977-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California-San Francisco, Department of Biochemistry and Biophysics, 513 Parnassus Avenue, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10320381" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Phosphatase/metabolism ; Amino Acid Substitution ; Cell Nucleus/*metabolism ; Cyclin-Dependent Kinases/metabolism ; Cyclins/metabolism ; *DNA-Binding Proteins ; Fungal Proteins/genetics/*metabolism ; *Homeodomain Proteins ; Karyopherins ; *Membrane Transport Proteins ; Nuclear Localization Signals ; Phosphorylation ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Trans-Activators/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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  • 13
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    Posttranscriptional gene silencing in Neurospora by a RecQ DNA helicase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: The phenomenon of posttranscriptional gene silencing (PTGS), which occurs when a transgene is introduced into a cell, is poorly understood. Here, the qde-3 gene, which is required for the activation and maintenance of gene silencing in the fungus Neurospora crassa, was isolated. Sequence analysis revealed that the qde-3 gene belongs to the RecQ DNA helicase family. The QDE3 protein may function in the DNA-DNA interaction between introduced transgenes or with an endogenous gene required for gene-silencing activation. In animals, genes that are homologous to RecQ protein, such as the human genes for Bloom's syndrome and Werner's syndrome, may also function in PTGS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cogoni, C -- Macino, G -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2342-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dipartimento di Biotecnologie Cellulari ed Ematologia, Sezione di Genetica Molecolare, Universita di Roma La Sapienza, Viale Regina Elena, 324, 00161 Roma, Italy. carlo@bce.med.uniroma1.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600745" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry/genetics/*metabolism ; Amino Acid Sequence ; Bloom Syndrome/genetics ; Camptothecin/pharmacology ; DNA Helicases/chemistry/genetics/*metabolism ; DNA, Fungal/metabolism ; Enzyme Inhibitors/pharmacology ; Etoposide/pharmacology ; *Fungal Proteins ; *Gene Silencing ; Genes, Fungal ; Genetic Complementation Test ; Humans ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Insertional ; Neurospora crassa/drug effects/enzymology/*genetics ; RecQ Helicases ; Sequence Alignment ; Transcription, Genetic ; Transgenes ; Werner Syndrome/genetics
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  • 14
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    Seeking ligands for lonely orphan receptors (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-06-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gustafsson, J A -- New York, N.Y. -- Science. 1999 May 21;284(5418):1285-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Nutrition, Karolinska Institutet, NOVUM Huddinge Hospital, Huddinge, Sweden. jan-ake.gustafsson@mednut.ki.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10383308" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bile Acids and Salts/biosynthesis ; Chenodeoxycholic Acid/*metabolism ; Cholesterol/*metabolism ; Cholesterol 7-alpha-Hydroxylase/biosynthesis/*genetics ; Cholic Acid/metabolism ; Cytochrome P-450 Enzyme System/metabolism ; DNA-Binding Proteins/*metabolism ; Fatty Acids/metabolism ; Gene Expression Regulation, Enzymologic ; Homeostasis ; Humans ; Ligands ; Liver/metabolism ; Mice ; Orphan Nuclear Receptors ; Receptors, Cytoplasmic and Nuclear/*metabolism ; Steroid Hydroxylases/metabolism ; Transcription Factors/*metabolism ; Transcription, Genetic
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  • 15
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    Genetic mechanisms of age regulation of human blood coagulation factor IX (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-31
    Description: Blood coagulation capacity increases with age in healthy individuals. Through extensive longitudinal analyses of human factor IX gene expression in transgenic mice, two essential age-regulatory elements, AE5' and AE3', have been identified. These elements are required and together are sufficient for normal age regulation of factor IX expression. AE5', a PEA-3 related element present in the 5' upstream region of the gene encoding factor IX, is responsible for age-stable expression of the gene. AE3', in the middle of the 3' untranslated region, is responsible for age-associated elevation in messenger RNA levels. In a concerted manner, AE5' and AE3' recapitulate natural patterns of the advancing age-associated increase in factor IX gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurachi, S -- Deyashiki, Y -- Takeshita, J -- Kurachi, K -- AG13283/AG/NIA NIH HHS/ -- HL38644/HL/NHLBI NIH HHS/ -- HL53713/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1999 Jul 30;285(5428):739-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, University of Michigan Medical School, Ann Arbor, MI 48109-0618, USA. kkurachi@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10426997" target="_blank"〉PubMed〈/a〉
    Keywords: *3' Untranslated Regions ; Aging/blood/*genetics ; Animals ; Consensus Sequence ; DNA Footprinting ; Dinucleotide Repeats ; Factor IX/*genetics/metabolism ; Female ; *Gene Expression Regulation ; Genetic Vectors ; Humans ; Male ; Mice ; Mice, Transgenic ; RNA, Messenger/genetics/metabolism ; *Regulatory Sequences, Nucleic Acid ; Transcription Factors/genetics/metabolism ; Transcription, Genetic ; Tumor Cells, Cultured
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  • 16
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    Sex and repression (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuroda, M I -- Kelley, R L -- New York, N.Y. -- Science. 1999 Jun 11;284(5421):1787-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA. mkuroda@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10391797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/embryology/*genetics/physiology ; *Caenorhabditis elegans Proteins ; *DNA-Binding Proteins ; Disorders of Sex Development ; *Dosage Compensation, Genetic ; Helminth Proteins/genetics/*physiology ; Male ; Regulatory Sequences, Nucleic Acid ; Repressor Proteins/genetics/*physiology ; *Sex Determination Processes ; Transcription, Genetic ; X Chromosome/*genetics/metabolism
    Print ISSN: 0036-8075
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  • 17
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    Three-dimensional structure of the human TFIID-IIA-IIB complex (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-11
    Description: The multisubunit transcription factor IID (TFIID) is an essential component of the eukaryotic RNA polymerase II machinery that works in concert with TFIIA (IIA) and TFIIB (IIB) to assemble initiation complexes at core eukaryotic promoters. Here the structures of human TFIID and the TFIID-IIA-IIB complex that were obtained by electron microscopy and image analysis to 35 angstrom resolution are presented. TFIID is a trilobed, horseshoe-shaped structure, with TFIIA and TFIIB bound on opposite lobes and flanking a central cavity. Antibody studies locate the TATA-binding protein (TBP) between TFIIA and TFIIB at the top of the cavity that most likely encompasses the TATA DNA binding region of the supramolecular complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andel, F 3rd -- Ladurner, A G -- Inouye, C -- Tjian, R -- Nogales, E -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2153-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10591646" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; DNA/metabolism ; DNA-Binding Proteins/chemistry/metabolism ; HeLa Cells ; Humans ; Image Processing, Computer-Assisted ; Microscopy, Electron ; Promoter Regions, Genetic ; Protein Conformation ; Recombinant Proteins/chemistry/metabolism ; TATA-Box Binding Protein ; Transcription Factor TFIIA ; Transcription Factor TFIIB ; Transcription Factor TFIID ; Transcription Factors/*chemistry/metabolism ; Transcription Factors, TFII/*chemistry/metabolism ; Transcription, Genetic
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    Polyploidy--more is more or less (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hieter, P -- Griffiths, T -- New York, N.Y. -- Science. 1999 Jul 9;285(5425):210-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics, University of British Columbia, Vancouver, British Columbia, Canada. hieter@cmmt.ubc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10428719" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle ; Cell Differentiation ; Cell Nucleus/metabolism ; Cyclins/genetics ; *Gene Expression Regulation, Fungal ; Meiosis ; Membrane Glycoproteins ; Membrane Proteins/genetics ; Mitosis ; Oligonucleotide Array Sequence Analysis ; *Polyploidy ; Saccharomyces cerevisiae/cytology/*genetics/physiology ; Saccharomyces cerevisiae Proteins ; Transcription, Genetic
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  • 19
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    Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-31
    Description: The generation of cell-mediated immunity against many infectious pathogens involves the production of interleukin-12 (IL-12), a key signal of the innate immune system. Yet, for many pathogens, the molecules that induce IL-12 production by macrophages and the mechanisms by which they do so remain undefined. Here it is shown that microbial lipoproteins are potent stimulators of IL-12 production by human macrophages, and that induction is mediated by Toll-like receptors (TLRs). Several lipoproteins stimulated TLR-dependent transcription of inducible nitric oxide synthase and the production of nitric oxide, a powerful microbicidal pathway. Activation of TLRs by microbial lipoproteins may initiate innate defense mechanisms against infectious pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brightbill, H D -- Libraty, D H -- Krutzik, S R -- Yang, R B -- Belisle, J T -- Bleharski, J R -- Maitland, M -- Norgard, M V -- Plevy, S E -- Smale, S T -- Brennan, P J -- Bloom, B R -- Godowski, P J -- Modlin, R L -- New York, N.Y. -- Science. 1999 Jul 30;285(5428):732-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Howard Hughes Medical Institute, University of California Los Angeles School of Medicine, Los Anges, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10426995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Bacterial/chemistry/*immunology/metabolism ; Cell Line ; *Drosophila Proteins ; Gene Expression Regulation ; Humans ; Interleukin-12/*biosynthesis/genetics ; Lipopolysaccharides/immunology ; Lipoproteins/chemistry/*immunology/metabolism ; Macrophages/*immunology/metabolism ; Membrane Glycoproteins/*metabolism ; Mice ; Monocytes/*immunology/metabolism ; Mycobacterium tuberculosis/*immunology ; NF-kappa B/biosynthesis ; Nitric Oxide Synthase/genetics ; Nitric Oxide Synthase Type II ; Promoter Regions, Genetic ; Receptors, Cell Surface/*metabolism ; Signal Transduction ; Toll-Like Receptors ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured
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  • 20
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    Single-molecule biomechanics with optical methods (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-12
    Description: Single-molecule observation and manipulation have come of age. With the advent of optical tweezers and other methods for probing and imaging single molecules, investigators have circumvented the model-dependent extrapolation from ensemble assays that has been the hallmark of classical biochemistry and biophysics. In recent years, there have been important advances in the understanding of how motor proteins work. The range of these technologies has also started to expand into areas such as DNA transcription and protein folding. Here, recent experiments with rotary motors, linear motors, RNA polymerase, and titin are described.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mehta, A D -- Rief, M -- Spudich, J A -- Smith, D A -- Simmons, R M -- New York, N.Y. -- Science. 1999 Mar 12;283(5408):1689-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry B400, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10073927" target="_blank"〉PubMed〈/a〉
    Keywords: Biomechanical Phenomena ; DNA/chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Flagella/chemistry/physiology ; Kinesin/chemistry/metabolism ; Lasers ; Microtubules/metabolism ; Molecular Motor Proteins/*chemistry/metabolism ; Muscle Proteins/*chemistry/metabolism ; Nucleic Acid Conformation ; Protein Conformation ; Protein Folding ; Proton-Translocating ATPases/chemistry/metabolism ; Transcription, Genetic
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  • 21
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    Evidence for autoregulation of cystathionine gamma-synthase mRNA stability in Arabidopsis (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-13
    Description: Control of messenger RNA (mRNA) stability serves as an important mechanism for regulating gene expression. Analysis of Arabidopsis mutants that overaccumulate soluble methionine (Met) revealed that the gene for cystathionine gamma-synthase (CGS), the key enzyme in Met biosynthesis, is regulated at the level of mRNA stability. Transfection experiments with wild-type and mutant forms of the CGS gene suggest that an amino acid sequence encoded by the first exon of CGS acts in cis to destabilize its own mRNA in a process that is activated by Met or one of its metabolites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiba, Y -- Ishikawa, M -- Kijima, F -- Tyson, R H -- Kim, J -- Yamamoto, A -- Nambara, E -- Leustek, T -- Wallsgrove, R M -- Naito, S -- New York, N.Y. -- Science. 1999 Nov 12;286(5443):1371-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10558994" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*enzymology/genetics ; Carbon-Oxygen Lyases/chemistry/*genetics/metabolism ; Exons ; Gene Expression Regulation, Enzymologic ; *Gene Expression Regulation, Plant ; Genes, Plant ; Genes, Reporter ; Kinetics ; Methionine/metabolism ; Molecular Sequence Data ; Mutation ; RNA, Messenger/genetics/*metabolism ; Sequence Alignment ; Transcription, Genetic ; Transfection
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  • 22
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    Identification of a mating type-like locus in the asexual pathogenic yeast Candida albicans (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-24
    Description: Candida albicans, the most prevalent fungal pathogen in humans, is thought to lack a sexual cycle. A set of C. albicans genes has been identified that corresponds to the master sexual cycle regulators a1, alpha1, and alpha2 of the Saccharomyces cerevisiae mating-type (MAT) locus. The C. albicans genes are arranged in a way that suggests that these genes are part of a mating type-like locus that is similar to the mating-type loci of other fungi. In addition to the transcriptional regulators a1, alpha1, and alpha2, the C. albicans mating type-like locus contains several genes not seen in other fungal MAT loci, including those encoding proteins similar to poly(A) polymerases, oxysterol binding proteins, and phosphatidylinositol kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hull, C M -- Johnson, A D -- GM37049/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 20;285(5431):1271-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10455055" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Phosphatidylinositol 4-Kinase/genetics ; Amino Acid Sequence ; Candida albicans/chemistry/*genetics/physiology ; Gene Deletion ; *Gene Expression Regulation, Fungal ; *Genes, Fungal ; *Genes, Mating Type, Fungal ; Homeodomain Proteins/chemistry/*genetics/metabolism ; Introns ; Molecular Sequence Data ; Open Reading Frames ; Operator Regions, Genetic ; Polynucleotide Adenylyltransferase/genetics ; Receptors, Steroid/genetics ; Recombination, Genetic ; Repressor Proteins/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae/chemistry/genetics ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic ; Transformation, Genetic
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  • 23
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    Global transposon mutagenesis and a minimal Mycoplasma genome (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-11
    Description: Mycoplasma genitalium with 517 genes has the smallest gene complement of any independently replicating cell so far identified. Global transposon mutagenesis was used to identify nonessential genes in an effort to learn whether the naturally occurring gene complement is a true minimal genome under laboratory growth conditions. The positions of 2209 transposon insertions in the completely sequenced genomes of M. genitalium and its close relative M. pneumoniae were determined by sequencing across the junction of the transposon and the genomic DNA. These junctions defined 1354 distinct sites of insertion that were not lethal. The analysis suggests that 265 to 350 of the 480 protein-coding genes of M. genitalium are essential under laboratory growth conditions, including about 100 genes of unknown function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hutchison, C A -- Peterson, S N -- Gill, S R -- Cline, R T -- White, O -- Fraser, C M -- Smith, H O -- Venter, J C -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2165-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Institute for Genomic Research, 9712 Medical Center Drive, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10591650" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/genetics/metabolism ; Amino Acyl-tRNA Synthetases/genetics ; Bacterial Proteins/genetics ; Chromosome Mapping ; DNA Polymerase III/genetics/metabolism ; DNA Replication/genetics ; *DNA Transposable Elements ; *Genes, Essential ; *Genome, Bacterial ; Glycolysis/genetics ; Lipoproteins/genetics ; *Mutagenesis, Insertional ; Mycoplasma/*genetics/metabolism ; Mycoplasma pneumoniae/genetics/metabolism ; Ribosomal Proteins/genetics ; Transcription, Genetic
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  • 24
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    Coordinate regulation of RAG1 and RAG2 by cell type-specific DNA elements 5' of RAG2 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-14
    Description: RAG1 and RAG2 are essential for V(D)J recombination and lymphocyte development. These genes are thought to encode a transposase derived from a mobile genetic element that was inserted into the vertebrate genome 450 million years ago. The regulation of RAG1 and RAG2 was investigated in vivo with bacterial artificial chromosome (BAC) transgenes containing a fluorescent indicator. Coordinate expression of RAG1 and RAG2 in B and T cells was found to be regulated by distinct genetic elements found on the 5' side of the RAG2 gene. This observation suggests a mechanism by which asymmetrically disposed cis DNA elements could influence the expression of the primordial transposon and thereby capture RAGs for vertebrate evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, W -- Misulovin, Z -- Suh, H -- Hardy, R R -- Jankovic, M -- Yannoutsos, N -- Nussenzweig, M C -- GM07739/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1080-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10446057" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*metabolism ; Bacterial Proteins/genetics ; DNA-Binding Proteins/*genetics ; *Gene Expression Regulation ; Genes, Immunoglobulin ; *Genes, RAG-1 ; Green Fluorescent Proteins ; Luminescent Proteins/genetics ; Mice ; Mice, Transgenic ; Recombinant Fusion Proteins ; Recombination, Genetic ; *Regulatory Sequences, Nucleic Acid ; Sequence Deletion ; T-Lymphocytes/*metabolism ; Transcription, Genetic ; Transgenes ; Transposases/genetics
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  • 25
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    Interlocked feedback loops within the Drosophila circadian oscillator (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-10-26
    Description: Drosophila Clock (dClk) is rhythmically expressed, with peaks in mRNA and protein (dCLK) abundance early in the morning. dClk mRNA cycling is shown here to be regulated by PERIOD-TIMELESS (PER-TIM)-mediated release of dCLK- and CYCLE (CYC)-dependent repression. Lack of both PER-TIM derepression and dCLK-CYC repression results in high levels of dClk mRNA, which implies that a separate dClk activator is present. These results demonstrate that the Drosophila circadian feedback loop is composed of two interlocked negative feedback loops: a per-tim loop, which is activated by dCLK-CYC and repressed by PER-TIM, and a dClk loop, which is repressed by dCLK-CYC and derepressed by PER-TIM.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glossop, N R -- Lyons, L C -- Hardin, P E -- NS-31214/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):766-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Biochemistry and Biological Clocks Program, University of Houston, Houston, TX 77204-5513, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10531060" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; CLOCK Proteins ; *Circadian Rhythm ; Dimerization ; Drosophila/*genetics/metabolism ; *Drosophila Proteins ; Feedback ; *Gene Expression Regulation ; Genes, Insect ; Insect Proteins/genetics ; Models, Genetic ; Mutation ; Nuclear Proteins/metabolism ; Period Circadian Proteins ; RNA, Messenger/genetics/metabolism ; Transcription Factors/*genetics/metabolism ; Transcription, Genetic
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  • 26
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    Recruitment of a hedgehog regulatory circuit in butterfly eyespot evolution (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-01-23
    Description: The origin of new morphological characters is a long-standing problem in evolutionary biology. Novelties arise through changes in development, but the nature of these changes is largely unknown. In butterflies, eyespots have evolved as new pattern elements that develop from special organizers called foci. Formation of these foci is associated with novel expression patterns of the Hedgehog signaling protein, its receptor Patched, the transcription factor Cubitus interruptus, and the engrailed target gene that break the conserved compartmental restrictions on this regulatory circuit in insect wings. Redeployment of preexisting regulatory circuits may be a general mechanism underlying the evolution of novelties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keys, D N -- Lewis, D L -- Selegue, J E -- Pearson, B J -- Goodrich, L V -- Johnson, R L -- Gates, J -- Scott, M P -- Carroll, S B -- F32 GM18162/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 1999 Jan 22;283(5401):532-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Laboratory of Molecular Biology, University of Wisconsin, 1525 Linden Drive, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9915699" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Body Patterning ; Butterflies/anatomy & histology/*genetics/growth & development ; DNA-Binding Proteins/genetics/physiology ; *Drosophila Proteins ; *Gene Expression Regulation ; Genes, Insect ; Hedgehog Proteins ; Homeodomain Proteins/genetics/physiology ; Insect Proteins/*genetics/physiology ; Membrane Proteins/genetics/physiology ; Pigmentation ; Receptors, Cell Surface ; Signal Transduction ; Transcription Factors/genetics/physiology ; Transcription, Genetic ; Wings, Animal/anatomy & histology/*growth & development/metabolism
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    Expansion of the allelic exclusion principle? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chess, A -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2067-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. chess@wi.mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9537917" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Animals ; CD4-Positive T-Lymphocytes/*immunology ; DNA Replication ; *Gene Expression Regulation ; Genes, Immunoglobulin ; Interleukin-2/*genetics ; Lymphocyte Activation ; Mice ; Polymerase Chain Reaction ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; Transcription, Genetic
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    Triplet-repeat transcripts: a role for DNA in disease (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, R H -- New York, N.Y. -- Science. 1998 May 1;280(5364):696-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Structural Biology, Institute for Molecular Medicine, Albert Einstein College of Medicine, Bronx, NY 10461, USA. rhsinger@aecom.yu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9599147" target="_blank"〉PubMed〈/a〉
    Keywords: CELF1 Protein ; Cell Nucleus/metabolism ; Exons ; Humans ; Models, Genetic ; Myotonic Dystrophy/*genetics/metabolism ; Myotonin-Protein Kinase ; Protein Binding ; Protein-Serine-Threonine Kinases/*genetics ; *RNA Splicing ; RNA, Messenger/*genetics ; RNA-Binding Proteins/genetics/*metabolism ; Ribonucleoproteins/genetics/*metabolism ; Transcription, Genetic ; Transfection ; *Trinucleotide Repeats ; Troponin/genetics ; Troponin T
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    Memory suppressor genes: inhibitory constraints on the storage of long-term memory (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: Synaptic plasticity, the ability of neurons to alter the strength of their synaptic connections with activity and experience, is thought to play a critical role in memory storage. Molecular studies of gene expression during long-lasting synaptic plasticity related to memory storage initially focused on the identification of positive regulators. More recent work has revealed that the establishment of long-lasting synaptic plasticity and long-term memory also requires the removal of inhibitory constraints. By analogy to tumor suppressor genes, which restrain cell proliferation, we propose that these inhibitory constraints of memory storage, which restrain synapse growth, be termed memory suppressor genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abel, T -- Martin, K C -- Bartsch, D -- Kandel, E R -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):338-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Center for Neurobiology and Behavior, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454331" target="_blank"〉PubMed〈/a〉
    Keywords: Activating Transcription Factor 2 ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Adhesion Molecules/physiology ; Cyclic AMP Response Element-Binding Protein/physiology ; Cyclic AMP-Dependent Protein Kinases/metabolism ; *Genes ; Memory/*physiology ; *Nerve Tissue Proteins ; Neuronal Plasticity/*genetics ; *Repressor Proteins ; Synapses/*physiology ; Transcription Factors/physiology ; Transcription, Genetic
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    BRCA1 required for transcription-coupled repair of oxidative DNA damage (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-14
    Description: The breast and ovarian cancer susceptibility gene BRCA1 encodes a zinc finger protein of unknown function. Association of the BRCA1 protein with the DNA repair protein Rad51 and changes in the phosphorylation and cellular localization of the protein after exposure to DNA-damaging agents are consistent with a role for BRCA1 in DNA repair. Here, it is shown that mouse embryonic stem cells deficient in BRCA1 are defective in the ability to carry out transcription-coupled repair of oxidative DNA damage, and are hypersensitive to ionizing radiation and hydrogen peroxide. These results suggest that BRCA1 participates, directly or indirectly, in transcription-coupled repair of oxidative DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gowen, L C -- Avrutskaya, A V -- Latour, A M -- Koller, B H -- Leadon, S A -- CA40453/CA/NCI NIH HHS/ -- CA70490/CA/NCI NIH HHS/ -- IP50CA58223/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 14;281(5379):1009-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Curriculum in Genetics and Molecular Biology and Department of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9703501" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; BRCA1 Protein/genetics/*physiology ; Cell Line ; DNA Damage ; *DNA Repair ; Hydrogen Peroxide ; Mice ; Oxidation-Reduction ; Stem Cells ; Thymine/analogs & derivatives/immunology/metabolism ; Transcription, Genetic ; Ultraviolet Rays
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    Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: Analysis of the 1,042,519-base pair Chlamydia trachomatis genome revealed unexpected features related to the complex biology of chlamydiae. Although chlamydiae lack many biosynthetic capabilities, they retain functions for performing key steps and interconversions of metabolites obtained from their mammalian host cells. Numerous potential virulence-associated proteins also were characterized. Several eukaryotic chromatin-associated domain proteins were identified, suggesting a eukaryotic-like mechanism for chlamydial nucleoid condensation and decondensation. The phylogenetic mosaic of chlamydial genes, including a large number of genes with phylogenetic origins from eukaryotes, implies a complex evolution for adaptation to obligate intracellular parasitism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stephens, R S -- Kalman, S -- Lammel, C -- Fan, J -- Marathe, R -- Aravind, L -- Mitchell, W -- Olinger, L -- Tatusov, R L -- Zhao, Q -- Koonin, E V -- Davis, R W -- AI 39258/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):754-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Infectious Diseases, University of California, Berkeley, CA 94720, USA. ctgenome@socrates.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784136" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Amino Acid Sequence ; Amino Acids/biosynthesis ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Proteins/chemistry/genetics ; Biological Evolution ; Chlamydia trachomatis/classification/*genetics/metabolism/physiology ; DNA Repair ; Energy Metabolism ; Enzymes/chemistry/genetics ; *Genome, Bacterial ; Humans ; Lipids/biosynthesis ; Molecular Sequence Data ; Peptidoglycan/biosynthesis/genetics ; Phylogeny ; Protein Biosynthesis ; Recombination, Genetic ; *Sequence Analysis, DNA ; Transcription, Genetic ; Transformation, Bacterial ; Virulence
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    RNAi in C. elegans: soaking in the genome sequence (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tabara, H -- Grishok, A -- Mello, C C -- DK32520-15/DK/NIDDK NIH HHS/ -- R01 HD33769-01/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):430-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841401" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; *Gene Expression Regulation ; *Genes, Helminth ; Mutation ; Phenotype ; RNA, Antisense/*genetics ; RNA, Double-Stranded/genetics ; RNA, Helminth/*genetics ; RNA, Messenger/genetics ; Transcription, Genetic
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    Reconstitution of peptide bond formation with Escherichia coli 23S ribosomal RNA domains (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-31
    Description: It was recently demonstrated that peptide bond formation can occur using an Escherichia coli naked 23S ribosomal RNA without any of the ribosomal proteins. Here, the six domains of the 23S ribosomal RNA were individually synthesized and shown to be capable, when complexed together, of stimulating the reaction. Omission and addition experiments indicated that the activity could be reconstituted solely by domain V at a concentration 10 times higher than that of the intact 23S ribosomal RNA, whereas domain VI could enhance the activity in trans. These findings suggest that fragments of an RNA molecule have the ability to associate into a functional whole.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nitta, I -- Kamada, Y -- Noda, H -- Ueda, T -- Watanabe, K -- New York, N.Y. -- Science. 1998 Jul 31;281(5377):666-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9685252" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Escherichia coli/*metabolism ; Neomycin/pharmacology ; Nucleic Acid Conformation ; *Peptide Biosynthesis ; Peptidyl Transferases/*metabolism ; Protein Synthesis Inhibitors/pharmacology ; RNA, Bacterial/chemistry/metabolism ; RNA, Ribosomal, 23S/chemistry/*metabolism ; RNA, Transfer, Amino Acyl/*metabolism ; Sparsomycin/pharmacology ; Transcription, Genetic
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    Heterocyst pattern formation controlled by a diffusible peptide (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-30
    Description: Many filamentous cyanobacteria grow as multicellular organisms that show a developmental pattern of single nitrogen-fixing heterocysts separated by approximately 10 vegetative cells. Overexpression of a 54-base-pair gene, patS, blocked heterocyst differentiation in Anabaena sp. strain PCC 7120. A patS null mutant showed an increased frequency of heterocysts and an abnormal pattern. Expression of a patS-gfp reporter was localized in developing proheterocysts. The addition of a synthetic peptide corresponding to the last five amino acids of PatS inhibited heterocyst development. PatS appears to control heterocyst pattern formation through intercellular signaling mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoon, H S -- Golden, J W -- GM36890/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):935-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Texas A&M University, College Station, TX 77843-3258, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9794762" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anabaena/cytology/genetics/*growth & development/metabolism ; Bacterial Proteins/chemistry/genetics/*physiology ; Base Sequence ; Cosmids ; Culture Media ; Diffusion ; Genes, Bacterial ; Genes, Reporter ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation, Missense ; Nitrates/metabolism ; Nitrogen Fixation ; Oligopeptides/pharmacology ; Peptide Fragments/pharmacology ; Phenotype ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transcription, Genetic
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    CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-04
    Description: Recruitment of the coactivator, CREB binding protein (CBP), by signal-regulated transcription factors, such as CREB [adenosine 3', 5'-monophosphate (cAMP) response element binding protein], is critical for stimulation of gene expression. The mouse pituitary cell line AtT20 was used to show that the CBP recruitment step (CREB phosphorylation on serine-133) can be uncoupled from CREB/CBP-activated transcription. CBP was found to contain a signal-regulated transcriptional activation domain that is controlled by nuclear calcium and calcium/calmodulin-dependent (CaM) protein kinase IV and by cAMP. Cytoplasmic calcium signals that stimulate the Ras mitogen-activated protein kinase signaling cascade or expression of the activated form of Ras provided the CBP recruitment signal but did not increase CBP activity and failed to activate CREB- and CBP-mediated transcription. These results identify CBP as a signal-regulated transcriptional coactivator and define a regulatory role for nuclear calcium and cAMP in CBP-dependent gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chawla, S -- Hardingham, G E -- Quinn, D R -- Bading, H -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1505-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9727976" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CREB-Binding Protein ; Calcium/*metabolism ; Calcium Channels/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Cell Line ; Cell Nucleus/*metabolism ; Cyclic AMP/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Cytoplasm/metabolism ; Genes, Reporter ; Mice ; Models, Genetic ; Nuclear Proteins/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Trans-Activators/*metabolism ; Transcription, Genetic ; *Transcriptional Activation ; ras Proteins/metabolism
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    p53-independent role of MDM2 in TGF-beta1 resistance (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: Transforming growth factor-beta (TGF-beta) inhibits cell proliferation, and acquisition of TGF-beta resistance has been linked to tumorigenesis. A genetic screen was performed to identify complementary DNAs that abrogated TGF-beta sensitivity in mink lung epithelial cells. Ectopic expression of murine double minute 2 rescued TGF-beta-induced growth arrest in a p53-independent manner by interference with retinoblastoma susceptibility gene product (Rb)/E2F function. In human breast tumor cells, increased MDM2 expression levels correlated with TGF-beta resistance. Thus, MDM2 may confer TGF-beta resistance in a subset of tumors and may promote tumorigenesis by interference with two independent tumor suppressors, p53 and Rb.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, P -- Dong, P -- Dai, K -- Hannon, G J -- Beach, D -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2270-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856953" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/genetics/metabolism/pathology ; *Carrier Proteins ; *Cell Cycle Proteins ; *Cell Division ; Cell Line ; Cell Transformation, Neoplastic ; *DNA-Binding Proteins ; Drug Resistance, Neoplasm ; E2F Transcription Factors ; Gene Expression ; Genes, Retinoblastoma ; Genes, p53 ; Genetic Vectors ; Humans ; Mice ; Mink ; *Nuclear Proteins ; Phosphorylation ; Proto-Oncogene Proteins/genetics/*physiology ; Proto-Oncogene Proteins c-mdm2 ; Retinoblastoma Protein/metabolism ; Retinoblastoma-Binding Protein 1 ; Signal Transduction ; Transcription Factor DP1 ; Transcription Factors/genetics/metabolism ; Transcription, Genetic ; Transforming Growth Factor beta/*pharmacology/physiology ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/*physiology
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    Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-10
    Description: The Rad53 protein kinase of Saccharomyces cerevisiae is required for checkpoints that prevent cell division in cells with damaged or incompletely replicated DNA. The Rad9 protein was phosphorylated in response to DNA damage, and phosphorylated Rad9 interacted with the COOH-terminal forkhead homology-associated (FHA) domain of Rad53. Inactivation of this domain abolished DNA damage-dependent Rad53 phosphorylation, G2/M cell cycle phase arrest, and increase of RNR3 transcription but did not affect replication inhibition-dependent Rad53 phosphorylation. Thus, Rad53 integrates DNA damage signals by coupling with phosphorylated Rad9. The hitherto uncharacterized FHA domain appears to be a modular protein-binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, Z -- Hsiao, J -- Fay, D S -- Stern, D F -- New York, N.Y. -- Science. 1998 Jul 10;281(5374):272-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9657725" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Cycle Proteins ; Checkpoint Kinase 2 ; *DNA Damage ; DNA Replication/drug effects ; Fungal Proteins/*metabolism ; G2 Phase ; Hydroxyurea/pharmacology ; Methyl Methanesulfonate/pharmacology ; Mitosis ; Mutation ; Oligopeptides ; Peptides ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; Saccharomyces cerevisiae/cytology/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic
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    Droplet discovery (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikorski, R -- Peters, R -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):412-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454334" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/metabolism ; DNA-Binding Proteins/metabolism ; *Drug Design ; *Genetic Techniques ; Heat-Shock Proteins/metabolism ; Microspheres ; Receptors, Transforming Growth Factor beta/metabolism ; Saccharomyces cerevisiae/*genetics ; Tacrolimus/pharmacology ; Tacrolimus Binding Proteins ; Transcription, Genetic
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    Capturing genes (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikorski, R -- Peters, R -- New York, N.Y. -- Science. 1997 Dec 19;278(5346):2143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9432723" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Complementary/*genetics ; Genes, myc ; *Genetic Techniques ; *Molecular Probe Techniques ; Polymerase Chain Reaction ; Protein Biosynthesis ; Puromycin ; RNA, Messenger/genetics ; Ribosomes/metabolism ; Transcription, Genetic
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    Monoallelic expression of the interleukin-2 locus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: The lymphokine interleukin-2 (IL-2) is responsible for autocrine cell cycle progression and regulation of immune responses. Uncontrolled secretion of IL-2 results in adverse reactions ranging from anergy, to aberrant T cell activation, to autoimmunity. With the use of fluorescent in situ hybridization and single-cell polymerase chain reaction in cells with different IL-2 alleles, IL-2 expression in mature thymocytes and T cells was found to be tightly controlled by monoallelic expression. Because IL-2 is encoded at a nonimprinted autosomal locus, this result represents an unusual regulatory mode for controlling the precise expression of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hollander, G A -- Zuklys, S -- Morel, C -- Mizoguchi, E -- Mobisson, K -- Simpson, S -- Terhorst, C -- Wishart, W -- Golan, D E -- Bhan, A K -- Burakoff, S J -- P01 CA39542-09/CA/NCI NIH HHS/ -- R01 AI17258-18/AI/NIAID NIH HHS/ -- R01 DK47677/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2118-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pediatric Immunology, Department of Research and Children's Hospital, Basel University Medical School, 4031 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9516115" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Animals ; CD4-Positive T-Lymphocytes/cytology/*immunology ; Concanavalin A/pharmacology ; DNA Replication ; Female ; Flow Cytometry ; *Gene Expression Regulation ; Heterozygote ; In Situ Hybridization, Fluorescence ; Interleukin-2/biosynthesis/*genetics ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred C57BL ; Muridae ; Mutation ; Polymerase Chain Reaction ; S Phase ; Transcription, Genetic
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    Structure of the amino-terminal protein interaction domain of STAT-4 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: STATs (signal transducers and activators of transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. The crystal structure of an NH2-terminal conserved domain (N-domain) comprising the first 123 residues of STAT-4 was determined at 1.45 angstroms. The domain consists of eight helices that are assembled into a hook-like structure. The N-domain has been implicated in several protein-protein interactions affecting transcription, and it enables dimerized STAT molecules to polymerize and to bind DNA cooperatively. The structure shows that N-domains can interact through an extensive interface formed by polar interactions across one face of the hook. Mutagenesis of an invariant tryptophan residue at the heart of this interface abolished cooperative DNA binding by the full-length protein in vitro and reduced the transcriptional response after cytokine stimulation in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vinkemeier, U -- Moarefi, I -- Darnell, J E Jr -- Kuriyan, J -- AI32489/AI/NIAID NIH HHS/ -- AI34420/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1048-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology and Laboratories of Molecular Biophysics, The Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461439" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Crystallography, X-Ray ; DNA/metabolism ; DNA-Binding Proteins/*chemistry/genetics/metabolism ; Humans ; Hydrogen Bonding ; Interferon-gamma/pharmacology ; Models, Molecular ; Molecular Sequence Data ; Oligodeoxyribonucleotides/metabolism ; *Protein Conformation ; Protein Structure, Tertiary ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; Signal Transduction ; Trans-Activators/*chemistry/genetics/metabolism ; Transcription, Genetic ; Transfection ; src Homology Domains
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    HIV-1 regulatory/accessory genes: keys to unraveling viral and host cell biology (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-25
    Description: Human immunodeficiency virus type-1 (HIV-1) manipulates fundamental host cell processes in sophisticated ways to achieve optimum replicative efficiency. Recent studies have provided new details on the molecular interactions of HIV-1 with its host cell. For example, HIV-1 encodes a protein that regulates transcriptional elongation by interacting with a cellular cyclin-dependent kinase, another that activates the specific nuclear export of viral RNA, and several others that affect the intracellular trafficking of viral and host cell proteins. Detailed analysis of the interplay between these viral proteins and normal cellular activities has provided new insights into central questions of virology and host cell biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Emerman, M -- Malim, M H -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1880-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Medicine, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North-Mailstop C2-023, Seattle, Washington 98109-1024, USA. memerman@fhcrc.org.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9632380" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Gene Products, nef/physiology ; Gene Products, rev/physiology ; Gene Products, tat/physiology ; *Genes, Viral ; HIV Infections/*virology ; HIV-1/*genetics/physiology ; Human Immunodeficiency Virus Proteins ; Humans ; Membrane Proteins/metabolism ; RNA, Viral/genetics/metabolism ; Trans-Activators/genetics/*physiology ; Transcription, Genetic ; Viral Regulatory and Accessory Proteins/genetics/*physiology ; nef Gene Products, Human Immunodeficiency Virus ; rev Gene Products, Human Immunodeficiency Virus ; tat Gene Products, Human Immunodeficiency Virus
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    A signaling complex of Ca2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Stimulation of T lymphocytes results in a rapid increase in intracellular calcium concentration ([Ca2+]i) that parallels the activation of Ca2+-calmodulin-dependent protein kinase IV (CaMKIV), a nuclear enzyme that can phosphorylate and activate the cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB). However, inactivation of CaMKIV occurs despite the sustained increase in [Ca2+]i that is required for T cell activation. A stable and stoichiometric complex of CaMKIV with protein serine-threonine phosphatase 2A (PP2A) was identified in which PP2A dephosphorylates CaMKIV and functions as a negative regulator of CaMKIV signaling. In Jurkat T cells, inhibition of PP2A activity by small t antigen enhanced activation of CREB-mediated transcription by CaMKIV. These findings reveal an intracellular signaling mechanism whereby a protein serine-threonine kinase (CaMKIV) is regulated by a tightly associated protein serine-threonine phosphatase (PP2A).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westphal, R S -- Anderson, K A -- Means, A R -- Wadzinski, B E -- GM33976/GM/NIGMS NIH HHS/ -- GM51366/GM/NIGMS NIH HHS/ -- HD07503/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 22;280(5367):1258-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596578" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Polyomavirus Transforming/metabolism ; Brain/enzymology ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/isolation & ; purification/*metabolism ; Calmodulin/metabolism ; Coenzymes/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Enzyme Activation ; Humans ; Jurkat Cells ; Lymphocyte Activation ; Mutation ; Phosphoprotein Phosphatases/isolation & purification/*metabolism ; Phosphorylation ; Protein Phosphatase 2 ; Rats ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/*enzymology ; Transcription, Genetic
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    Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: Myotonic dystrophy (DM) is caused by a CTG expansion in the 3' untranslated region of the DM gene. One model of DM pathogenesis suggests that RNAs from the expanded allele create a gain-of-function mutation by the inappropriate binding of proteins to the CUG repeats. Data presented here indicate that the conserved heterogeneous nuclear ribonucleoprotein, CUG-binding protein (CUG-BP), may mediate the trans-dominant effect of the RNA. CUG-BP was found to bind to the human cardiac troponin T (cTNT) pre-messenger RNA and regulate its alternative splicing. Splicing of cTNT was disrupted in DM striated muscle and in normal cells expressing transcripts that contain CUG repeats. Altered expression of genes regulated posttranscriptionally by CUG-BP therefore may contribute to DM pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philips, A V -- Timchenko, L T -- Cooper, T A -- AR 44387/AR/NIAMS NIH HHS/ -- HL45565/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 May 1;280(5364):737-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563950" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; CELF1 Protein ; Cell Line ; Cell Nucleus/metabolism ; Exons ; Humans ; Introns ; Muscle, Skeletal/cytology/embryology/metabolism ; Mutation ; Myotonic Dystrophy/*genetics/metabolism ; Myotonin-Protein Kinase ; Phosphorylation ; Protein-Serine-Threonine Kinases/*genetics ; RNA Precursors/metabolism ; RNA, Messenger/*genetics/metabolism ; RNA-Binding Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Ribonucleoproteins/genetics/*metabolism ; Transcription, Genetic ; Transfection ; *Trinucleotide Repeats ; Troponin/genetics ; Troponin T
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    Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-04
    Description: Cyanobacteria are the simplest organisms known to have a circadian clock. A circadian clock gene cluster kaiABC was cloned from the cyanobacterium Synechococcus. Nineteen clock mutations were mapped to the three kai genes. Promoter activities upstream of the kaiA and kaiB genes showed circadian rhythms of expression, and both kaiA and kaiBC messenger RNAs displayed circadian cycling. Inactivation of any single kai gene abolished these rhythms and reduced kaiBC-promoter activity. Continuous kaiC overexpression repressed the kaiBC promoter, whereas kaiA overexpression enhanced it. Temporal kaiC overexpression reset the phase of the rhythms. Thus, a negative feedback control of kaiC expression by KaiC generates a circadian oscillation in cyanobacteria, and KaiA sustains the oscillation by enhancing kaiC expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ishiura, M -- Kutsuna, S -- Aoki, S -- Iwasaki, H -- Andersson, C R -- Tanabe, A -- Golden, S S -- Johnson, C H -- Kondo, T -- MH01179/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1519-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan. ishiura@bio.nagoya-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9727980" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics ; Biological Clocks/*genetics ; Circadian Rhythm/*genetics ; Circadian Rhythm Signaling Peptides and Proteins ; Cloning, Molecular ; Cyanobacteria/*genetics/physiology ; Feedback ; *Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Genes, Reporter ; Luminescence ; Models, Biological ; Molecular Sequence Data ; Multigene Family ; Mutation ; Promoter Regions, Genetic ; Recombinant Fusion Proteins ; Transcription, Genetic
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    Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-31
    Description: The cerebral cortex of Alzheimer's and Down syndrome patients is characterized by the presence of protein deposits in neurofibrillary tangles, neuritic plaques, and neuropil threads. These structures were shown to contain forms of beta amyloid precursor protein and ubiquitin-B that are aberrant (+1 proteins) in the carboxyl terminus. The +1 proteins were not found in young control patients, whereas the presence of ubiquitin-B+1 in elderly control patients may indicate early stages of neurodegeneration. The two species of +1 proteins displayed cellular colocalization, suggesting a common origin, operating at the transcriptional level or by posttranscriptional editing of RNA. This type of transcript mutation is likely an important factor in the widely occurring nonfamilial early- and late-onset forms of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Leeuwen, F W -- de Kleijn, D P -- van den Hurk, H H -- Neubauer, A -- Sonnemans, M A -- Sluijs, J A -- Koycu, S -- Ramdjielal, R D -- Salehi, A -- Martens, G J -- Grosveld, F G -- Peter, J -- Burbach, H -- Hol, E M -- New York, N.Y. -- Science. 1998 Jan 9;279(5348):242-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School for Neurosciences Amsterdam, Netherlands Institute for Brain Research, 1105 AZ Amsterdam, The Netherlands. f.van.leeuwen@nih.knaw.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9422699" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aging/genetics ; Alzheimer Disease/*genetics/metabolism/pathology ; Amino Acid Sequence ; Amyloid beta-Protein Precursor/analysis/chemistry/*genetics ; Base Sequence ; *Brain Chemistry ; Cerebral Cortex/chemistry/pathology ; Cloning, Molecular ; Down Syndrome/*genetics/metabolism/pathology ; Female ; *Frameshift Mutation ; Hippocampus/chemistry/pathology ; Humans ; Male ; Molecular Sequence Data ; Neurites/chemistry ; Neurofibrillary Tangles/chemistry ; Neuropil/chemistry ; Polymerase Chain Reaction ; RNA Editing ; Repetitive Sequences, Nucleic Acid ; Sequence Deletion ; Transcription, Genetic ; Ubiquitins/analysis/chemistry/*genetics/metabolism
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    How cyanobacteria count to 10 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haselkorn, R -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):891-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA. r-haselkorn@uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841437" target="_blank"〉PubMed〈/a〉
    Keywords: Anabaena/cytology/genetics/*growth & development/metabolism ; Bacterial Proteins/chemistry/genetics/metabolism/*physiology ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Mutation ; Nitrogen Fixation ; Oligopeptides/metabolism/pharmacology ; Plant Proteins/genetics/metabolism ; Promoter Regions, Genetic ; Signal Transduction ; Transcription Factors/metabolism ; Transcription, Genetic
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    Identification of c-MYC as a target of the APC pathway (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-04
    Description: The adenomatous polyposis coli gene (APC) is a tumor suppressor gene that is inactivated in most colorectal cancers. Mutations of APC cause aberrant accumulation of beta-catenin, which then binds T cell factor-4 (Tcf-4), causing increased transcriptional activation of unknown genes. Here, the c-MYC oncogene is identified as a target gene in this signaling pathway. Expression of c-MYC was shown to be repressed by wild-type APC and activated by beta-catenin, and these effects were mediated through Tcf-4 binding sites in the c-MYC promoter. These results provide a molecular framework for understanding the previously enigmatic overexpression of c-MYC in colorectal cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, T C -- Sparks, A B -- Rago, C -- Hermeking, H -- Zawel, L -- da Costa, L T -- Morin, P J -- Vogelstein, B -- Kinzler, K W -- CA57345/CA/NCI NIH HHS/ -- CA62924/CA/NCI NIH HHS/ -- GM07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1509-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Johns Hopkins Oncology Center, 424 North Bond Street, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9727977" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Binding Sites ; Cell Line ; Colorectal Neoplasms/*genetics ; Cytoskeletal Proteins/genetics/metabolism ; *Gene Expression Regulation, Neoplastic ; *Genes, APC ; Genes, Reporter ; *Genes, myc ; HT29 Cells ; Humans ; Mutation ; Promoter Regions, Genetic ; Proto-Oncogene Proteins c-myc/metabolism ; Signal Transduction ; TCF Transcription Factors ; *Trans-Activators ; Transcription Factor 7-Like 2 Protein ; Transcription Factors/metabolism ; Transcription, Genetic ; beta Catenin
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    Complete genome sequence of Treponema pallidum, the syphilis spirochete (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-17
    Description: The complete genome sequence of Treponema pallidum was determined and shown to be 1,138,006 base pairs containing 1041 predicted coding sequences (open reading frames). Systems for DNA replication, transcription, translation, and repair are intact, but catabolic and biosynthetic activities are minimized. The number of identifiable transporters is small, and no phosphoenolpyruvate:phosphotransferase carbohydrate transporters were found. Potential virulence factors include a family of 12 potential membrane proteins and several putative hemolysins. Comparison of the T. pallidum genome sequence with that of another pathogenic spirochete, Borrelia burgdorferi, the agent of Lyme disease, identified unique and common genes and substantiates the considerable diversity observed among pathogenic spirochetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, C M -- Norris, S J -- Weinstock, G M -- White, O -- Sutton, G G -- Dodson, R -- Gwinn, M -- Hickey, E K -- Clayton, R -- Ketchum, K A -- Sodergren, E -- Hardham, J M -- McLeod, M P -- Salzberg, S -- Peterson, J -- Khalak, H -- Richardson, D -- Howell, J K -- Chidambaram, M -- Utterback, T -- McDonald, L -- Artiach, P -- Bowman, C -- Cotton, M D -- Fujii, C -- Garland, S -- Hatch, B -- Horst, K -- Roberts, K -- Sandusky, M -- Weidman, J -- Smith, H O -- Venter, J C -- AI31068/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):375-88.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, Rockville, MD 20850, USA. tpdb@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9665876" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/metabolism ; Base Sequence ; Borrelia burgdorferi Group/genetics ; Carrier Proteins/genetics/metabolism ; DNA Repair/genetics ; DNA Replication/genetics ; DNA Restriction Enzymes/genetics ; Energy Metabolism/genetics ; Genes, Bacterial ; Genes, Regulator ; *Genome, Bacterial ; Heat-Shock Response/genetics ; Lipoproteins/genetics ; Membrane Proteins/genetics ; Molecular Sequence Data ; Movement ; Open Reading Frames ; Oxygen Consumption/genetics ; Protein Biosynthesis ; Recombination, Genetic ; Replication Origin ; *Sequence Analysis, DNA ; Transcription, Genetic ; Treponema pallidum/*genetics/metabolism/pathogenicity
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    Genetic variation as a guide to drug development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleyn, P W -- Vesell, E S -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1820-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Millennium Predictive Medicine, Inc., Cambridge, MA 02139-4815, USA. kleyn@mpi.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776686" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; *Chemistry, Pharmaceutical ; Genetic Linkage ; Genetic Markers ; *Genetic Variation ; Genotype ; Humans ; Microsatellite Repeats ; *Pharmacogenetics ; Polymorphism, Genetic ; Transcription, Genetic
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    Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: Integrin-mediated reorganization of cell shape leads to an altered cellular phenotype. Disruption of the actin cytoskeleton, initiated by binding of soluble antibody to alpha5beta1 integrin, led to increased expression of the collagenase-1 gene in rabbit synovial fibroblasts. Activation of the guanosine triphosphate-binding protein Rac1, which was downstream of the integrin, was necessary for this process, and expression of activated Rac1 was sufficient to increase expression of collagenase-1. Rac1 activation generated reactive oxygen species that were essential for nuclear factor kappa B-dependent transcriptional regulation of interleukin-1alpha, which, in an autocrine manner, induced collagenase-1 gene expression. Remodeling of the extracellular matrix and consequent alterations of integrin-mediated adhesion and cytoarchitecture are central to development, wound healing, inflammation, and malignant disease. The resulting activation of Rac1 may lead to altered gene regulation and alterations in cellular morphogenesis, migration, and invasion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kheradmand, F -- Werner, E -- Tremble, P -- Symons, M -- Werb, Z -- AR20684/AR/NIAMS NIH HHS/ -- DE10306/DE/NIDCR NIH HHS/ -- HL03732/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 8;280(5365):898-902.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco, CA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9572733" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; *Cell Size ; Collagenases/*genetics ; Cytochalasin D/pharmacology ; Enzyme Activation ; Fibroblasts ; Free Radicals ; GTP Phosphohydrolases/genetics/*metabolism ; GTP-Binding Proteins/genetics/*metabolism ; *Gene Expression Regulation, Enzymologic ; Genes, Reporter ; Hydrogen Peroxide ; Interleukin-1/genetics/metabolism ; Matrix Metalloproteinase 1 ; NF-kappa B/metabolism ; Rabbits ; Reactive Oxygen Species/*metabolism ; Receptors, Fibronectin/physiology ; Transcription, Genetic ; rac GTP-Binding Proteins
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  • 52
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    Role of ceruloplasmin in cellular iron uptake (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-21
    Description: Individuals with hereditary ceruloplasmin (Cp) deficiency have profound iron accumulation in most tissues, which suggests that Cp is important for normal release of cellular iron. Here, in contrast to expectations, Cp was shown to increase iron uptake by HepG2 cells, increasing the apparent affinity for the substrate by three times. Consistent with its role in iron uptake, Cp synthesis was regulated by iron supply and was increased four- to fivefold after iron depletion. Unlike other iron controllers that are posttranscriptionally regulated, Cp synthesis was transcriptionally regulated. Thus, iron-deficient cells could increase Cp synthesis to maintain intracellular iron homeostasis, so that defects would lead to global accumulation of iron in tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mukhopadhyay, C K -- Attieh, Z K -- Fox, P L -- HL29582/HL/NHLBI NIH HHS/ -- HL52692/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 30;279(5351):714-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, The Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9445478" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Ceruloplasmin/biosynthesis/genetics/pharmacology/*physiology ; Chlorides ; Culture Media, Conditioned ; Ferric Compounds/pharmacology ; Homeostasis ; Humans ; Iron/*metabolism ; Iron Chelating Agents/pharmacology ; Liver/metabolism ; RNA, Messenger/genetics/metabolism ; Transcription, Genetic ; Transferrin/metabolism ; Tumor Cells, Cultured
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    Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: The nuclear factor of activated T cells (NFAT) group of transcription factors is retained in the cytoplasm of quiescent cells. NFAT activation is mediated in part by induced nuclear import. This process requires calcium-dependent dephosphorylation of NFAT caused by the phosphatase calcineurin. The c-Jun amino-terminal kinase (JNK) phosphorylates NFAT4 on two sites. Mutational removal of the JNK phosphorylation sites caused constitutive nuclear localization of NFAT4. In contrast, JNK activation in calcineurin-stimulated cells caused nuclear exclusion of NFAT4. These findings show that the nuclear accumulation of NFAT4 promoted by calcineurin is opposed by the JNK signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chow, C W -- Rincon, M -- Cavanagh, J -- Dickens, M -- Davis, R J -- CA58396/CA/NCI NIH HHS/ -- CA65831/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1638-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374467" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; COS Cells ; Calcineurin/metabolism ; Calcineurin Inhibitors ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cell Nucleus/*metabolism ; Cyclosporine/pharmacology ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Mutation ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphorylation ; Protein Kinases/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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  • 54
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    Immune hyperactivation of HIV-1-infected T cells mediated by Tat and the CD28 pathway (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-07
    Description: Human immunodeficiency virus-type 1 (HIV-1) infection is characterized by a chronic state of immune hyperactivation in patients. Infection of human peripheral blood lymphocytes with HIV-1 in vitro resulted in increased interleukin-2 (IL-2) secretion in response to T cell activation via the CD3 and CD28 receptors. Expression of the HIV-1 transactivator Tat recapitulated this phenotype and was associated with increased IL-2 secretion in response to costimulation with CD3 plus CD28. IL-2 superinduction by Tat occurred at the transcriptional level, was mediated by the CD28-responsive element in the IL-2 promoter, and was exclusively dependent on the 29 amino acids encoded by the second exon of Tat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ott, M -- Emiliani, S -- Van Lint, C -- Herbein, G -- Lovett, J -- Chirmule, N -- McCloskey, T -- Pahwa, S -- Verdin, E -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1481-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Picower Institute for Medical Research, 350 Community Drive, Manhasset, NY 11030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9045614" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/pharmacology ; Antibodies, Monoclonal/immunology ; Antigens, CD28/*immunology ; Antigens, CD3/immunology ; Exons ; Gene Products, tat/genetics/*physiology ; HIV Infections/immunology ; HIV-1/drug effects/genetics/*physiology ; Humans ; Interleukin-2/genetics/*secretion ; Jurkat Cells ; Leukocytes, Mononuclear/virology ; *Lymphocyte Activation ; Promoter Regions, Genetic ; T-Lymphocytes/*immunology/*virology ; Transcription Factors/metabolism ; Transcription, Genetic ; Transfection ; Zidovudine/pharmacology ; tat Gene Products, Human Immunodeficiency Virus
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    Macromolecular trafficking indicated by localization and turnover of sucrose transporters in enucleate sieve elements (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-28
    Description: The leaf sucrose transporter SUT1 is essential for phloem loading and long-distance transport of assimilates. Both SUT1 messenger RNA (mRNA) and protein were shown to be diurnally regulated and to have high turnover rates. SUT1 protein was detected by immunolocalization in plasma membranes of enucleate sieve elements (SEs) in tobacco, potato, and tomato. Analysis by in situ hybridization showed that SUT1 mRNA localizes mainly to the SE and is preferentially associated with plasmodesmata. Antisense inhibition of SUT1 expression under control of a companion cell (CC)-specific promoter indicated synthesis of SUT1 mRNA in the CC. These results provide evidence for targeting of plant endogenous mRNA and potentially SUT1 protein through phloem plasmodesmata and for sucrose loading at the plasma membrane of SE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, C -- Franceschi, V R -- Schulz, A -- Lemoine, R -- Frommer, W B -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1298-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Botanik, Eberhard-Karls-Universitat, Auf der Morgenstelle 1, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036853" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport, Active ; Carrier Proteins/analysis/genetics/*metabolism ; Cell Membrane/chemistry/metabolism ; Fluorescent Antibody Technique ; Immunohistochemistry ; In Situ Hybridization ; Lycopersicon esculentum/metabolism ; Membrane Proteins/analysis/genetics/*metabolism ; *Membrane Transport Proteins ; Molecular Sequence Data ; Plant Leaves/chemistry/cytology/*metabolism ; Plant Proteins/analysis/genetics/*metabolism ; Plants, Toxic ; RNA, Messenger/analysis/genetics/metabolism ; RNA, Plant/analysis/genetics/metabolism ; Solanum tuberosum ; Sucrose/metabolism ; Tobacco/metabolism ; Transcription, Genetic
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    Ribozymes in wonderland (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellington, A D -- Robertson, M P -- Bull, J -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):546-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148415" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; DNA-Directed RNA Polymerases/genetics/metabolism ; *Directed Molecular Evolution ; Evolution, Molecular ; *RNA, Catalytic/chemistry/genetics/metabolism ; Selection, Genetic ; Transcription, Genetic ; Viral Proteins
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    Continuous in vitro evolution of catalytic function (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: A population of RNA molecules that catalyze the template-directed ligation of RNA substrates was made to evolve in a continuous manner in the test tube. A simple serial transfer procedure was used to achieve approximately 300 successive rounds of catalysis and selective amplification in 52 hours. During this time, the population size was maintained against an overall dilution of 3 x 10(298). Both the catalytic rate and amplification rate of the RNAs improved substantially as a consequence of mutations that accumulated during the evolution process. Continuous in vitro evolution makes it possible to maintain laboratory "cultures" of catalytic molecules that can be perpetuated indefinitely.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wright, M C -- Joyce, G F -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):614-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9110984" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; DNA-Directed RNA Polymerases/genetics/metabolism ; *Directed Molecular Evolution ; Evolution, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; *RNA, Catalytic/chemistry/genetics/metabolism ; Saccharomyces cerevisiae/chemistry ; Templates, Genetic ; Transcription, Genetic ; Viral Proteins
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    Researchers get their first good look at the nucleosome (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Featherstone, C -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1763-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9324764" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; Crystallography, X-Ray ; DNA/*chemistry ; Histones/*chemistry ; Models, Molecular ; Nucleic Acid Conformation ; Nucleosomes/*chemistry ; *Protein Conformation ; Protein Folding ; Transcription, Genetic
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  • 59
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    The origin recognition complex, SIR1, and the S phase requirement for silencing (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-06
    Description: Silencing of transcription in Saccharomyces cerevisiae has several links to DNA replication, including a role for the origin recognition complex (ORC), the DNA replication initiator, in both processes. In addition, the establishment of silencing at the HML and HMR loci requires cells to pass through the S phase of the cell cycle. Passage through S phase was required for silencing of HMR even under conditions in which ORC itself was no longer required. The requirement for ORC in silencing of HMR could be bypassed by tethering the Sir1 protein to the HMR-E silencer. However, ORC had a Sir1-independent role in transcriptional silencing at telomeres. Thus, the role of ORC in silencing was separable from its role in initiation, and the role of S phase in silencing was independent of replication initiation at the silencers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, C A -- Ehrenhofer-Murray, A E -- Loo, S -- Rine, J -- GM31105/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 6;276(5318):1547-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, Division of Genetics, 401 Barker Hall, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9171055" target="_blank"〉PubMed〈/a〉
    Keywords: *Aldose-Ketose Isomerases ; Chromatin/physiology ; Chromosomes, Fungal/physiology ; *DNA Replication ; DNA, Fungal/genetics/physiology ; DNA-Binding Proteins/*physiology ; Fungal Proteins/genetics/*physiology ; *Gene Expression Regulation, Fungal ; Origin Recognition Complex ; Recombinant Fusion Proteins/genetics ; S Phase/*physiology ; Saccharomyces cerevisiae/cytology/*genetics ; *Saccharomyces cerevisiae Proteins ; *Silent Information Regulator Proteins, Saccharomyces cerevisiae ; Telomere ; Trans-Activators/genetics/*physiology ; Transcription, Genetic
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    NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: Activation of the nuclear factor of activated T cells transcription factor (NF-AT) is a key event underlying lymphocyte action. The CAML (calcium-modulator and cyclophilin ligand) protein is a coinducer of NF-AT activation when overexpressed in Jurkat T cells. A member of the tumor necrosis factor receptor superfamily was isolated by virtue of its affinity for CAML. Cross-linking of this lymphocyte-specific protein, designated TACI (transmembrane activator and CAML-interactor), on the surface of transfected Jurkat cells with TACI-specific antibodies led to activation of the transcription factors NF-AT, AP-1, and NFkappaB. TACI-induced activation of NF-AT was specifically blocked by a dominant-negative CAML mutant, thus implicating CAML as a signaling intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Bulow, G U -- Bram, R J -- CA21765/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Oncology, St. Jude Children's Research Hospital, 332 North Lauderdale, Memphis, TN 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311921" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Calcineurin ; Calmodulin-Binding Proteins/metabolism ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; DNA-Binding Proteins/*metabolism ; Humans ; Jurkat Cells ; Lymphocyte Activation ; *Membrane Proteins ; Molecular Sequence Data ; Mutation ; NF-kappa B/metabolism ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphoprotein Phosphatases/metabolism ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*metabolism ; Sequence Alignment ; Signal Transduction ; T-Lymphocytes/immunology/*metabolism ; Transcription Factor AP-1/metabolism ; Transcription Factors/*metabolism ; Transcription, Genetic ; Transfection ; Transmembrane Activator and CAML Interactor Protein
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    Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: The signal transduction pathway or pathways linking extracellular signals to myogenesis are poorly defined. Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. This indicates that muscle-specific gene expression is necessary but not sufficient to commit differentiated myocytes to myotubes and suggests a function for the MAPKs during the early and late stages of skeletal muscle differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, A M -- Tonks, N K -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Demerec Building, 1 Bungtown Road, Post Office Box 100, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360925" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Cell Cycle Proteins ; Cell Differentiation ; Cell Division ; Cell Line ; Cloning, Molecular ; Culture Media ; Cyclin D1/genetics ; Dual Specificity Phosphatase 1 ; Gene Expression Regulation, Developmental ; Immediate-Early Proteins/genetics/*metabolism ; JNK Mitogen-Activated Protein Kinases ; Mice ; Mitogen-Activated Protein Kinase 1/antagonists & inhibitors/*metabolism ; *Mitogen-Activated Protein Kinases ; Mitogens/pharmacology ; Muscle Proteins/*genetics ; Muscle, Skeletal/*cytology/*enzymology/metabolism ; *Phosphoprotein Phosphatases ; Phosphorylation ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Tetracycline/pharmacology ; Transcription, Genetic
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    Control of filament formation in Candida albicans by the transcriptional repressor TUP1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: The pathogenic yeast Candida albicans regulates its cellular morphology in response to environmental conditions. Ellipsoidal, single cells (blastospores) predominate in rich media, whereas filaments composed of elongated cells that are attached end-to-end form in response to starvation, serum, and other conditions. The TUP1 gene, which encodes a general transcriptional repressor in Saccharomyces cerevisiae, was isolated from C. albicans and disrupted. The resulting tup1 mutant strain of C. albicans grew exclusively as filaments under all conditions tested. TUP1 was epistatic to the transcriptional activator CPH1, previously found to promote filamentous growth. The results suggest a model where TUP1 represses genes responsible for initiating filamentous growth and this repression is lifted under inducing environmental conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Braun, B R -- Johnson, A D -- GM37049/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):105-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143-0414, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204892" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Candida albicans/*cytology/*genetics/growth & development/metabolism ; Cloning, Molecular ; Culture Media ; DNA-Binding Proteins/metabolism ; Epistasis, Genetic ; Fungal Proteins/chemistry/*genetics/*metabolism ; Gene Deletion ; Genes, Fungal ; Glycerol/metabolism ; Models, Genetic ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Phenotype ; Repressor Proteins/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Temperature ; Transcription Factors/metabolism ; Transcription, Genetic
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    Combinatorial control required for the specificity of yeast MAPK signaling (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-28
    Description: In yeast, an overlapping set of mitogen-activated protein kinase (MAPK) signaling components controls mating, haploid invasion, and pseudohyphal development. Paradoxically, a single downstream transcription factor, Ste12, is necessary for the execution of these distinct programs. Developmental specificity was found to require a transcription factor of the TEA/ATTS family, Tec1, which cooperates with Ste12 during filamentous and invasive growth. Purified derivatives of Ste12 and Tec1 bind cooperatively to enhancer elements called filamentation and invasion response elements (FREs), which program transcription that is specifically responsive to the MAPK signaling components required for filamentous growth. An FRE in the TEC1 promoter functions in a positive feedback loop required for pseudohyphal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Madhani, H D -- Fink, G R -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1314-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036858" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; *Enhancer Elements, Genetic ; Fungal Proteins/*metabolism ; Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase Kinases/metabolism ; Mitogen-Activated Protein Kinase Kinases ; Mutation ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Retroelements ; Saccharomyces cerevisiae/genetics/growth & development/*metabolism ; *Saccharomyces cerevisiae Proteins ; *Schizosaccharomyces pombe Proteins ; Signal Transduction ; *Transcription Factors ; Transcription, Genetic
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    Control of inflammation, cytokine expression, and germinal center formation by BCL-6 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: The gene encoding the BCL-6 transcriptional repressor is frequently translocated and mutated in diffuse large cell lymphoma. Mice with a disrupted BCL-6 gene developed myocarditis and pulmonary vasculitis, had no germinal centers, and had increased expression of T helper cell type 2 cytokines. The BCL-6 DNA recognition motif resembled sites bound by the STAT (signal transducers and activators of transcription) transcription factors, which mediate cytokine signaling. BCL-6 could repress interleukin-4 (IL-4)-induced transcription when bound to a site recognized by the IL-4-responsive transcription factor Stat6. Thus, dysregulation of STAT-responsive genes may underlie the inflammatory disease in BCL-6-deficient mice and participate in lymphoid malignancies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dent, A L -- Shaffer, A L -- Yu, X -- Allman, D -- Staudt, L M -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):589-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Metabolism Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9110977" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Cells, Cultured ; Cytokines/*biosynthesis ; DNA-Binding Proteins/genetics/*physiology ; Ficoll/analogs & derivatives/immunology ; Germinal Center/*immunology ; Hemocyanin/immunology ; Immunoglobulins/biosynthesis ; Inflammation/*immunology/pathology ; Interferon-gamma/biosynthesis ; Interleukin-4/metabolism ; Interleukins/biosynthesis/metabolism ; Lymphocyte Activation ; Mice ; Myocarditis/immunology/pathology ; Proto-Oncogene Proteins/genetics/*physiology ; Proto-Oncogene Proteins c-bcl-6 ; Receptors, IgE/genetics ; STAT6 Transcription Factor ; Signal Transduction ; Spleen/immunology ; T-Lymphocytes/immunology ; Th2 Cells/immunology ; Trans-Activators/metabolism ; Transcription Factors/genetics/*physiology ; Transcription, Genetic ; Trinitrobenzenes/immunology ; Vasculitis/immunology/pathology
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    Myc and Max homologs in Drosophila (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-29
    Description: The proteins encoded by the myc proto-oncogene family are involved in cell proliferation, apoptosis, differentiation, and neoplasia. Myc acts through dimerization with Max to bind DNA and activate transcription. Homologs of the myc and max genes were cloned from the fruit fly Drosophila melanogaster and their protein products (dMyc and dMax) were shown to heterodimerize, recognize the same DNA sequence as their vertebrate homologs, and activate transcription. The dMyc protein is likely encoded by the Drosophila gene diminutive (dm), a mutation in which results in small body size and female sterility caused by degeneration of the ovaries. These findings indicate a potential role for Myc in germ cell development and set the stage for genetic analysis of Myc and Max.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallant, P -- Shiio, Y -- Cheng, P F -- Parkhurst, S M -- Eisenman, R N -- R01CA47138/CA/NCI NIH HHS/ -- R01GM47852/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1523-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1124 Columbia Street, Seattle WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929412" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Cloning, Molecular ; DNA Transposable Elements ; DNA, Complementary ; DNA-Binding Proteins/chemistry/genetics/metabolism ; Dimerization ; *Drosophila Proteins ; Drosophila melanogaster/chemistry/*genetics/growth & development/metabolism ; Female ; Gene Expression Regulation, Developmental ; Genes, Insect ; Genes, myc ; *Helix-Loop-Helix Motifs ; Humans ; Molecular Sequence Data ; Oligonucleotide Probes/metabolism ; Ovary/metabolism ; Proto-Oncogene Proteins c-myc/chemistry/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic
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    Evidence that Spt6p controls chromatin structure by a direct interaction with histones (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-07
    Description: Genetic analysis has implicated SPT6, an essential gene of Saccharomyces cerevisiae, in the control of chromatin structure. Mutations in SPT6 and particular mutations in histone genes are able to overcome transcriptional defects in strains lacking the Snf/Swi protein complex. Here it is shown that an spt6 mutation causes changes in chromatin structure in vivo. In addition, both in vivo and in vitro experiments provide evidence that Spt6p interacts directly with histones and primarily with histone H3. Consistent with these findings, Spt6p is capable of nucleosome assembly in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bortvin, A -- Winston, F -- GM32967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1473-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633238" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/chemistry/genetics/metabolism/*ultrastructure ; DNA, Fungal/metabolism ; Fungal Proteins/genetics/metabolism/*physiology ; Histones/chemistry/genetics/*metabolism ; Humans ; Mutation ; Nuclear Proteins/genetics/metabolism/*physiology ; Nucleosomes/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic ; Transcriptional Elongation Factors
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    Molecular pathways controlling heart development (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: Heart formation requires complex interactions among cells from multiple embryonic origins. Recent studies have begun to reveal the genetic pathways that control cardiac morphogenesis. Many of the genes within these pathways are conserved across vast phylogenetic distances, which has allowed cardiac development to be dissected in organisms ranging from flies to mammals. Studies of cardiac development have also revealed the molecular defects underlying several congenital cardiac malformations in humans and may ultimately provide opportunities for genetic testing and intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, E N -- Srivastava, D -- New York, N.Y. -- Science. 1996 May 3;272(5262):671-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Oncology, University of Texas Southwestern Medical Center, Dallas, 75235-9148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; *Gene Expression Regulation, Developmental ; Genes ; Genes, Regulator ; Heart/*embryology ; Heart Conduction System/embryology ; Heart Defects, Congenital/embryology/*genetics/pathology ; Humans ; Morphogenesis ; Mutation ; Myocardium/cytology ; Neural Crest/cytology ; Transcription Factors/physiology ; Transcription, Genetic
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    Life's last domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1043-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8711482" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Chromosomes, Bacterial ; Cloning, Molecular ; DNA, Bacterial/*genetics ; Gene Library ; *Genome, Bacterial ; Methane/metabolism ; Methanococcus/classification/*genetics/physiology ; Pressure ; Protein Biosynthesis ; Sequence Analysis, DNA ; Temperature ; Transcription, Genetic
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    Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-23
    Description: The complete 1.66-megabase pair genome sequence of an autotrophic archaeon, Methanococcus jannaschii, and its 58- and 16-kilobase pair extrachromosomal elements have been determined by whole-genome random sequencing. A total of 1738 predicted protein-coding genes were identified; however, only a minority of these (38 percent) could be assigned a putative cellular role with high confidence. Although the majority of genes related to energy production, cell division, and metabolism in M. jannaschii are most similar to those found in Bacteria, most of the genes involved in transcription, translation, and replication in M. jannaschii are more similar to those found in Eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bult, C J -- White, O -- Olsen, G J -- Zhou, L -- Fleischmann, R D -- Sutton, G G -- Blake, J A -- FitzGerald, L M -- Clayton, R A -- Gocayne, J D -- Kerlavage, A R -- Dougherty, B A -- Tomb, J F -- Adams, M D -- Reich, C I -- Overbeek, R -- Kirkness, E F -- Weinstock, K G -- Merrick, J M -- Glodek, A -- Scott, J L -- Geoghagen, N S -- Venter, J C -- GM00783/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1058-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbiology Department, University of Illinois, Champaign-Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688087" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*genetics ; Base Composition ; Base Sequence ; Biological Transport/genetics ; Carbon Dioxide/metabolism ; Chromosome Mapping ; Chromosomes, Bacterial/genetics ; DNA Replication ; DNA, Bacterial/*genetics ; Databases, Factual ; Energy Metabolism/genetics ; Genes, Bacterial ; *Genome, Bacterial ; Hydrogen/metabolism ; Methane/metabolism ; Methanococcus/*genetics/physiology ; Molecular Sequence Data ; Protein Biosynthesis ; Sequence Analysis, DNA ; Transcription, Genetic
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    Homologous association of oppositely imprinted chromosomal domains (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: Human chromosome 15q11-q13 encompasses the Prader-Willi syndrome (PWS) and the Angelman syndrome (AS) loci, which are subject to parental imprinting, a process that marks the parental origin of certain chromosomal subregions. A temporal and spatial association between maternal and paternal chromosomes 15 was observed in human T lymphocytes by three-dimensional fluorescence in situ hybridization. This association occurred specifically at the imprinted 15q11-q13 regions only during the late S phase of the cell cycle. Cells from PWS and AS patients were deficient in association, which suggests that normal imprinting involves mutual recognition and preferential association of maternal and paternal chromosomes 15.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaSalle, J M -- Lalande, M -- R01 NS30628/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 May 3;272(5262):725-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Genetics Division, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614834" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Angelman Syndrome/*genetics ; Chromosomes, Human, Pair 15/*genetics/ultrastructure ; DNA/metabolism ; DNA Probes ; *Genomic Imprinting ; Humans ; In Situ Hybridization, Fluorescence ; Methylation ; Microscopy, Confocal ; Prader-Willi Syndrome/*genetics ; S Phase ; T-Lymphocytes/cytology/*ultrastructure ; Transcription, Genetic
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    An RNA polymerase II elongation factor encoded by the human ELL gene (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-29
    Description: The human ELL gene on chromosome 19 undergoes frequent translocations with the trithorax-like MLL gene on chromosome 11 in acute myeloid leukemias. Here, ELL was shown to encode a previously uncharacterized elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. Functionally, ELL resembles Elongin (SIII), a transcription elongation factor regulated by the product of the von Hippel-Lindau (VHL) tumor suppressor gene. The discovery of a second elongation factor implicated in oncogenesis provides further support for a close connection between the regulation of transcription elongation and cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shilatifard, A -- Lane, W S -- Jackson, K W -- Conaway, R C -- Conaway, J W -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1873-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City, 73104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596958" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/*genetics/metabolism ; Genes, Tumor Suppressor ; Histone-Lysine N-Methyltransferase ; Humans ; Leukemia/genetics ; Molecular Sequence Data ; Myeloid-Lymphoid Leukemia Protein ; *Neoplasm Proteins ; *Peptide Elongation Factors ; *Proto-Oncogenes ; RNA Polymerase II/*metabolism ; RNA, Messenger/genetics/metabolism ; Rats ; Recombinant Proteins/metabolism ; Transcription Factors/chemistry/*genetics/metabolism ; Transcription, Genetic ; Transcriptional Elongation Factors ; Translocation, Genetic ; von Hippel-Lindau Disease/genetics
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    Cell cycle regulation of E2F site occupation in vivo (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: DNA-binding E2F complexes have been identified throughout the mammalian cell cycle, including the transcriptionally inactive complexes with pocket proteins, which occur early in the prereplicative G1 phase of the cycle, and the transactivating free E2F, which increases in late G1. Here, a regulatory B-myb promoter site was shown to bind with high affinity to free E2F and to E2F-pocket protein complexes in an indistinguishable way in vitro. In contrast, in vivo footprinting with NIH 3T3 cells demonstrated E2F site occupation specifically in early G1, when the B-myb promoter is inactive. These observations indicate that a novel mechanism governs E2F-DNA interactions during the cell cycle and emphasize the relevance of E2F site-directed transcriptional repression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwicker, J -- Liu, N -- Engeland, K -- Lucibello, F C -- Muller, R -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1595-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Tumorforschung, Philipps-Universitat Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599118" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; *Carrier Proteins ; *Cell Cycle Proteins ; DNA/*metabolism ; DNA-Binding Proteins/*genetics/metabolism ; E2F Transcription Factors ; *G1 Phase ; Mice ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; *Promoter Regions, Genetic ; Retinoblastoma-Binding Protein 1 ; Retinoblastoma-Like Protein p107 ; *S Phase ; *Trans-Activators ; Transcription Factor DP1 ; Transcription Factors/*genetics/*metabolism ; Transcription, Genetic
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    Crystal structure of the yeast TFIIA/TBP/DNA complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-10
    Description: The crystal structure of the yeast TFIIA/TBP/TATA promoter complex was solved to 3 angstrom resolution by double-edge multiple wavelength anomalous diffraction from two different species of anomalous scattering elements in the same crystal. The large and small subunits of TFIIA associate intimately to form both domains of a two-domain folding pattern. TFIIA binds as a heterodimer to the side of the TBP/TATA complex opposite to the side that binds TFIIB and does not alter the TBP/DNA interaction. The six-stranded beta-sandwich domain interacts with the amino-terminal end of TBP through a stereospecific parallel beta-strand interface and with the backbone of the TATA box and the 5'-flanking B-DNA segment. The four-helix-bundle domain projects away from the TBP/TATA complex, thereby presenting a substantial surface for further protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiger, J H -- Hahn, S -- Lee, S -- Sigler, P B -- New York, N.Y. -- Science. 1996 May 10;272(5263):830-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629014" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Crystallography, X-Ray ; DNA, Fungal/*chemistry/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae/chemistry/genetics/metabolism ; TATA Box ; TATA-Box Binding Protein ; Transcription Factor TFIIA ; Transcription Factor TFIIB ; Transcription Factors/*chemistry/metabolism ; Transcription, Genetic
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    The shrewd grasp of RNA polymerase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landick, R -- Roberts, J W -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):202-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin, Madison, 53706-1567, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8668996" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; DNA/chemistry/*metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Escherichia coli/enzymology ; Nucleic Acid Conformation ; Protein Binding ; RNA, Messenger/*metabolism ; Templates, Genetic ; Transcription, Genetic ; Zinc Fingers
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    Transition in specification of embryonic metazoan DNA replication origins (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-10
    Description: In early Xenopus embryos, in which ribosomal RNA genes (rDNA) are not transcribed, rDNA replication initiates and terminates at 9- to 12-kilobase pair intervals, with no detectable dependence on specific DNA sequences. Resumption of ribosomal RNA (rRNA) synthesis at late blastula and early gastrula is accompanied by a specific repression of replication initiation within transcription units; the frequency of initiation within intergenic spacers remains as high as in early blastula. These results demonstrate that for rRNA genes, circumscribed zones of replication initiation emerge in intergenic DNA during the time in metazoan development when the chromatin is remodeled to allow gene transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hyrien, O -- Maric, C -- Mechali, M -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):994-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Jacques Monod, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481806" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/*metabolism ; *DNA Replication ; DNA, Ribosomal/*biosynthesis/genetics ; Gastrula/*metabolism ; RNA, Ribosomal/*biosynthesis/genetics ; *Replication Origin ; Transcription, Genetic ; Xenopus laevis
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    Induction of MHC class I genes in neurons (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-28
    Description: Whether neurons express major histocompatibility complex (MHC) class I genes has not been firmly established. The techniques of confocal laser microscopy, patch clamp electrophysiology, and reverse transcriptase-polymerase chain reaction were combined here to directly examine the inducibility of MHC class I genes in individual cultured rat hippocampal neurons. Transcription of MHC class I genes was very rare in neurons with spontaneous action potentials. In electrically silent neurons, transcription was noted, with expression of beta 2-microglobulin under tighter control than in class I heavy chain molecules. Surface expression of class I molecules occurred only in electrically silent neurons treated with interferon gamma. Immunosurveillance by cytotoxic T cells may be focused on functionally impaired neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neumann, H -- Cavalie, A -- Jenne, D E -- Wekerle, H -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):549-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroimmunology, Max Planck Institute for Psychiatry, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624779" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Animals ; Base Sequence ; Cells, Cultured ; *Gene Expression Regulation ; *Genes, MHC Class I ; Hippocampus/cytology ; Histocompatibility Antigens Class I/biosynthesis/genetics ; Interferon-gamma/pharmacology ; Molecular Sequence Data ; Patch-Clamp Techniques ; Polymerase Chain Reaction ; Pyramidal Cells/cytology/*metabolism/physiology ; RNA, Messenger/genetics/metabolism ; Rats ; Rats, Inbred Lew ; Tetrodotoxin/pharmacology ; Transcription, Genetic ; beta 2-Microglobulin/biosynthesis/genetics
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    Mapping the cell's nucleus (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baskin, Y -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1564-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777854" target="_blank"〉PubMed〈/a〉
    Keywords: *Gene Expression Regulation ; Nuclear Matrix/chemistry/*genetics/ultrastructure ; Nuclear Proteins/*physiology ; RNA Splicing ; RNA, Messenger/*genetics ; Transcription, Genetic
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    Circuit simulation of genetic networks (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-04
    Description: Genetic networks with tens to hundreds of genes are difficult to analyze with currently available techniques. Because of the many parallels in the function of these biochemically based genetic circuits and electrical circuits, a hybrid modeling approach is proposed that integrates conventional biochemical kinetic modeling within the framework of a circuit simulation. The circuit diagram of the bacteriophage lambda lysislysogeny decision circuit represents connectivity in signal paths of the biochemical components. A key feature of the lambda genetic circuit is that operons function as active integrated logic components and introduce signal time delays essential for the in vivo behavior of phage lambda.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McAdams, H H -- Shapiro, L -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):650-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Beckman Center, Stanford University School of Medicine 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624793" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriolysis ; Bacteriophage lambda/*genetics/physiology ; *Computer Simulation ; DNA Nucleotidyltransferases/genetics/metabolism ; *DNA-Binding Proteins ; Feedback ; *Gene Expression Regulation, Viral ; Integrases ; Lysogeny/*genetics ; Mathematics ; *Models, Genetic ; *Operon ; Promoter Regions, Genetic ; RNA, Messenger/genetics/metabolism ; RNA, Viral/genetics/metabolism ; Repressor Proteins/genetics/metabolism ; Signal Transduction ; Software ; Terminator Regions, Genetic ; Transcription Factors/genetics/metabolism ; Transcription, Genetic ; Viral Proteins/genetics/metabolism ; Viral Regulatory and Accessory Proteins ; Virus Activation ; Virus Integration
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    How the glucocorticoids suppress immunity (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):232-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569969" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Inflammatory Agents/pharmacology ; Cell Nucleus/metabolism ; DNA/metabolism ; DNA-Binding Proteins/biosynthesis/genetics/*metabolism ; Dexamethasone/pharmacology ; Glucocorticoids/*pharmacology ; Humans ; *I-kappa B Proteins ; *Immunosuppression ; Immunosuppressive Agents/*pharmacology ; NF-kappa B/*antagonists & inhibitors/metabolism ; Receptors, Glucocorticoid/metabolism ; Transcription, Genetic
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  • 80
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    Frequency and distribution of DNA uptake signal sequences in the Haemophilus influenzae Rd genome (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-28
    Description: The naturally transformable, Gram-negative bacterium Haemophilus influenzae Rd preferentially takes up DNA of its own species by recognizing a 9-base pair sequence, 5'-AAGTGCGGT, carried in multiple copies in its chromosome. With the availability of the complete genome sequence, 1465 copies of the 9-base pair uptake site have been identified. Alignment of these sites unexpectedly reveals an extended consensus region of 29 base pairs containing the core 9-base pair region and two downstream 6-base pair A/T-rich regions, each spaced about one helix turn apart. Seventeen percent of the sites are in inverted repeat pairs, many of which are located downstream to gene termini and are capable of forming stem-loop structures in messenger RNA that might function as signals for transcription termination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, H O -- Tomb, J F -- Dougherty, B A -- Fleischmann, R D -- Venter, J C -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):538-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542802" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Chromosome Mapping ; Consensus Sequence ; Conserved Sequence ; DNA, Bacterial/chemistry/*genetics ; Escherichia coli/genetics ; *Genome, Bacterial ; Haemophilus influenzae/*genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligonucleotide Probes ; RNA, Bacterial/chemistry/genetics ; RNA, Messenger/chemistry/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic ; *Transformation, Bacterial
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  • 81
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    Glucocorticoids (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ray, A -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1103.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502023" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Glucocorticoids/pharmacology ; Humans ; Interleukin-6/genetics ; NF-kappa B/*metabolism ; Receptors, Glucocorticoid/*metabolism ; Transcription, Genetic
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  • 82
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    Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-13
    Description: The Saccharomyces cerevisiae MATa1 and MAT alpha 2 homeodomain proteins, which play a role in determining yeast cell type, form a heterodimer that binds DNA and represses transcription in a cell type-specific manner. Whereas the alpha 2 and a1 proteins on their own have only modest affinity for DNA, the a1/alpha 2 heterodimer binds DNA with high specificity and affinity. The three-dimensional crystal structure of the a1/alpha 2 homeodomain heterodimer bound to DNA was determined at a resolution of 2.5 A. The a1 and alpha 2 homeodomains bind in a head-to-tail orientation, with heterodimer contacts mediated by a 16-residue tail located carboxyl-terminal to the alpha 2 homeodomain. This tail becomes ordered in the presence of a1, part of it forming a short amphipathic helix that packs against the a1 homeodomain between helices 1 and 2. A pronounced 60 degree bend is induced in the DNA, which makes possible protein-protein and protein-DNA contacts that could not take place in a straight DNA fragment. Complex formation mediated by flexible protein-recognition peptides attached to stably folded DNA binding domains may prove to be a general feature of the architecture of other classes of eukaryotic transcriptional regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, T -- Stark, M R -- Johnson, A D -- Wolberger, C -- GM-37049/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):262-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569974" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; DNA, Fungal/*chemistry/metabolism ; Fungal Proteins/*chemistry/metabolism ; Homeodomain Proteins/*chemistry/metabolism ; Hydrogen Bonding ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Operator Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Repressor Proteins/*chemistry/metabolism ; Saccharomyces cerevisiae/*chemistry/genetics ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic
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  • 83
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    The minimal gene complement of Mycoplasma genitalium (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: The complete nucleotide sequence (580,070 base pairs) of the Mycoplasma genitalium genome, the smallest known genome of any free-living organism, has been determined by whole-genome random sequencing and assembly. A total of only 470 predicted coding regions were identified that include genes required for DNA replication, transcription and translation, DNA repair, cellular transport, and energy metabolism. Comparison of this genome to that of Haemophilus influenzae suggests that differences in genome content are reflected as profound differences in physiology and metabolic capacity between these two organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, C M -- Gocayne, J D -- White, O -- Adams, M D -- Clayton, R A -- Fleischmann, R D -- Bult, C J -- Kerlavage, A R -- Sutton, G -- Kelley, J M -- Fritchman, R D -- Weidman, J F -- Small, K V -- Sandusky, M -- Fuhrmann, J -- Nguyen, D -- Utterback, T R -- Saudek, D M -- Phillips, C A -- Merrick, J M -- Tomb, J F -- Dougherty, B A -- Bott, K F -- Hu, P C -- Lucier, T S -- Peterson, S N -- Smith, H O -- Hutchison, C A 3rd -- Venter, J C -- AI33161/AI/NIAID NIH HHS/ -- AIO8998/AI/NIAID NIH HHS/ -- HL19171/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):397-403.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569993" target="_blank"〉PubMed〈/a〉
    Keywords: Antigenic Variation/genetics ; Bacterial Proteins/genetics ; Biological Transport/genetics ; DNA Repair/genetics ; DNA Replication/genetics ; DNA, Bacterial/genetics ; Databases, Factual ; Energy Metabolism/genetics ; Genes, Bacterial ; *Genome, Bacterial ; Haemophilus influenzae/genetics ; Molecular Sequence Data ; Mycoplasma/*genetics/immunology/metabolism ; Open Reading Frames ; Protein Biosynthesis ; *Sequence Analysis, DNA ; Transcription, Genetic
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  • 84
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    A heterodimeric transcriptional repressor becomes crystal clear (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andrews, B J -- Donoviel, M S -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):251-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Medical Genetics, University of Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569972" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; DNA, Fungal/chemistry/*metabolism ; Fungal Proteins/*chemistry/metabolism ; Homeodomain Proteins/*chemistry/metabolism ; Macromolecular Substances ; Nucleic Acid Conformation ; Operator Regions, Genetic ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Repressor Proteins/*chemistry/metabolism ; Saccharomyces cerevisiae/*chemistry/genetics ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic
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  • 85
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    Protein sculptors that help turn on genes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1587-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502065" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/metabolism ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/metabolism ; *Gene Expression Regulation ; Integration Host Factors ; Lymphoid Enhancer-Binding Factor 1 ; *Nuclear Proteins ; *Nucleic Acid Conformation ; Sex-Determining Region Y Protein ; Transcription Factors/chemistry/*metabolism ; Transcription, Genetic
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  • 86
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    Requirement for MAP kinase (ERK2) activity in interferon alpha- and interferon beta-stimulated gene expression through STAT proteins (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: Activation of early response genes by interferons (IFNs) requires tyrosine phosphorylation of STAT (signal transducers and activators of transcription) proteins. It was found that the serine-threonine kinase mitogen-activated protein kinase (MAPK) [specifically, the 42-kilodalton MAPK or extracellular signal-regulated kinase 2 (ERK2)] interacted with the alpha subunit of IFN-alpha/beta receptor in vitro and in vivo. Treatment of cells with IFN-beta induced tyrosine phosphorylation and activation of MAPK and caused MAPK and Stat1 alpha to coimmunoprecipitate. Furthermore, expression of dominant negative MAPK inhibited IFN-beta-induced transcription. Therefore, MAPK appears to regulate IFN-alpha and IFN-beta activation of early response genes by modifying the Jak-STAT signaling cascade.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉David, M -- Petricoin, E 3rd -- Benjamin, C -- Pine, R -- Weber, M J -- Larner, A C -- GM47332/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1721-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cytokine Biology, Center for Biologics Evaluation and Research, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569900" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cells, Cultured ; DNA-Binding Proteins/*metabolism ; Enzyme Activation ; *Gene Expression Regulation ; Humans ; Interferon-alpha/pharmacology ; Interferon-beta/*pharmacology ; Membrane Proteins ; Mitogen-Activated Protein Kinase 1 ; Phosphorylation ; Receptor, Interferon alpha-beta ; Receptors, Interferon/*metabolism ; Recombinant Fusion Proteins/metabolism ; STAT1 Transcription Factor ; *Signal Transduction ; Trans-Activators/*metabolism ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; Tyrosine/metabolism
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  • 87
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    Converting Escherichia coli RNA polymerase into an enhancer-responsive enzyme: role of an NH2-terminal leucine patch in sigma 54 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-10
    Description: The protein sigma 54 associates with Escherichia coli core RNA polymerase to form a holoenzyme that binds promoters but is inactive in the absence of enhancer activation. Here, mutants of sigma 54 enabled polymerases to transcribe without enhancer protein and adenosine triphosphate. The mutations are in leucines within the NH2-terminal glutamine-rich domain of sigma 54. Multiple leucine substitutions mimicked the effect of enhancer protein, which suggests that the enhancer protein functions to disrupt a leucine patch. The results indicate that sigma 54 acts both as an inhibitor of polymerase activity and as a receptor that interacts with enhancer protein to overcome this inhibition, and that these two activities jointly confer enhancer responsiveness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J T -- Syed, A -- Hsieh, M -- Gralla, J D -- GM35754/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):992-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481805" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacterial Proteins/physiology ; DNA-Binding Proteins/*physiology ; DNA-Directed RNA Polymerases/chemistry/genetics/*metabolism ; *Enhancer Elements, Genetic ; Escherichia coli/*enzymology/genetics/growth & development ; Escherichia coli Proteins ; Leucine/chemistry ; Molecular Sequence Data ; Mutation ; PII Nitrogen Regulatory Proteins ; Promoter Regions, Genetic ; RNA Polymerase Sigma 54 ; Sigma Factor/chemistry/genetics/*metabolism ; *Trans-Activators ; Transcription Factors/*physiology ; Transcription, Genetic
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  • 88
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    Requirement of RNA polymerase III transcription factors for in vitro position-specific integration of a retroviruslike element (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: The yeast retroviruslike element Ty3 inserts at the transcription initiation sites of genes transcribed by RNA polymerase III (Pol III). An in vitro integration assay was developed with the use of Ty3 viruslike particles and a modified SUP2 tyrosine transfer RNA (tRNA(Tyr)) gene target. Integration was position-specific and required Ty3 integrase, Pol III transcription factor (TF) IIIB-, TFIIIC-, and Pol III-containing fractions showed that TFIIIB and TFIIIC, together, were sufficient for position-specific Ty3 integration, but not for transcription. This report demonstrates that in vitro integration of a retroelement can be targeted by cellular proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kirchner, J -- Connolly, C M -- Sandmeyer, S B -- 33281/PHS HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1488-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878467" target="_blank"〉PubMed〈/a〉
    Keywords: DNA Nucleotidyltransferases/metabolism ; Integrases ; Models, Genetic ; Mutagenesis, Site-Directed ; RNA Polymerase III/*genetics ; RNA, Transfer, Tyr/genetics ; *Recombination, Genetic ; *Retroelements ; Saccharomyces cerevisiae/*genetics ; Transcription Factor TFIIIB ; Transcription Factors/*metabolism ; *Transcription Factors, TFIII ; Transcription, Genetic ; *Virus Integration
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  • 89
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    Altered DNA recognition and bending by insertions in the alpha 2 tail of the yeast a1/alpha 2 homeodomain heterodimer (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-13
    Description: The yeast MAT alpha 2 and MATa1 homeodomain proteins bind cooperatively as a heterodimer to sites upstream of haploid-specific genes, repressing their transcription. In the crystal structure of alpha 2 and a1 bound to DNA, each homeodomain makes independent base-specific contacts with the DNA and the two proteins contact each other through an extended tail region of alpha 2 that tethers the two homeodomains to one another. Because this extended region may be flexible, the ability of the heterodimer to discriminate among DNA sites with altered spacing between alpha 2 and a1 binding sites was examined. Spacing between the half sites was critical for specific DNA binding and transcriptional repression by the complex. However, amino acid insertions in the tail region of alpha 2 suppressed the effect of altering an a1/alpha 2 site by increasing the spacing between the half sites. Insertions in the tail also decreased DNA bending by a1/alpha 2. Thus tethering the two homeodomains contributes to DNA bending by a1/alpha 2, but the precise nature of the resulting bend is not essential for repression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jin, Y -- Mead, J -- Li, T -- Wolberger, C -- Vershon, A K -- GM49265/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):290-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855-0759, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569977" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Fungal/chemistry/genetics/*metabolism ; Fungal Proteins/chemistry/*metabolism ; Genes, Fungal ; Homeodomain Proteins/chemistry/*metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Mutagenesis, Insertional ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Repressor Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/chemistry ; *Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Transcription, Genetic
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  • 90
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    The neuron-restrictive silencer factor (NRSF): a coordinate repressor of multiple neuron-specific genes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-03
    Description: The neuron-restrictive silencer factor (NRSF) binds a DNA sequence element, called the neuron-restrictive silencer element (NRSE), that represses neuronal gene transcription in nonneuronal cells. Consensus NRSEs have been identified in 18 neuron-specific genes. Complementary DNA clones encoding a functional fragment of NRSF were isolated and found to encode a novel protein containing eight noncanonical zinc fingers. Expression of NRSF mRNA was detected in most nonneuronal tissues at several developmental stages. In the nervous system, NRSF mRNA was detected in undifferentiated neuronal progenitors, but not in differentiated neurons. NRSF represents the first example of a vertebrate silencer protein that potentially regulates a large battery of cell type-specific genes, and therefore may function as a master negative regulator of neurogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schoenherr, C J -- Anderson, D J -- NS23476/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1360-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 216-76, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871435" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain-Derived Neurotrophic Factor ; Cell Line ; Central Nervous System/chemistry/cytology/embryology ; DNA, Complementary/genetics ; DNA-Binding Proteins/analysis/chemistry/genetics/*physiology ; *Gene Expression Regulation ; Humans ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Mice ; Molecular Sequence Data ; Nerve Growth Factors/genetics ; Nerve Tissue Proteins/genetics ; Neurons/chemistry ; *Regulatory Sequences, Nucleic Acid ; Repressor Proteins/physiology ; Sodium Channels/genetics ; Stem Cells/chemistry ; Synapsins/genetics ; Transcription Factors/analysis/chemistry/genetics/*physiology ; Transcription, Genetic ; Transfection ; Zinc Fingers
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  • 91
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    Specific recognition of cruciform DNA by nuclear protein HMG1 (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-24
    Description: Cruciform DNA, a non-double helix form of DNA, can be generated as an intermediate in genetic recombination as well as from palindromic sequences under the effect of supercoiling. Eukaryotic cells are equipped with a DNA-binding protein that selectively recognizes cruciform DNA. Biochemical and immunological data showed that this protein is HMG1, an evolutionarily conserved, essential, and abundant component of the nucleus. The interaction with a ubiquitous protein points to a critical role for cruciform DNA conformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bianchi, M E -- Beltrame, M -- Paonessa, G -- New York, N.Y. -- Science. 1989 Feb 24;243(4894 Pt 1):1056-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Heidleberg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2922595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics/*metabolism ; Electrophoresis, Polyacrylamide Gel ; High Mobility Group Proteins/genetics/isolation & purification/*metabolism ; Immunoassay ; Immunoblotting ; Liver/analysis ; Molecular Sequence Data ; Molecular Weight ; *Nucleic Acid Conformation ; Peptide Fragments/genetics/isolation & purification ; Protein Biosynthesis ; Rats ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Kappa B-specific DNA binding proteins: role in the regulation of human interleukin-2 gene expression (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-28
    Description: Transcriptional activation of the human interleukin-2 (IL-2) gene, like induction of the IL-2 receptor alpha (IL-2R alpha) gene and the type 1 human immunodeficiency virus (HIV-1), is shown to be modulated by a kappa B-like enhancer element. Mutation of a kappa B core sequence identified in the IL-2 promoter (-206 to -195) partially inhibits both mitogen- and HTLV-I Tax-mediated activation of this transcription unit and blocks the specific binding of two inducible cellular factors. These kappa B-specific proteins (80 to 90 and 50 to 55 kilodaltons) similarly interact with the functional kappa B enhancer present in the IL-2R alpha promoter. These data suggest that these kappa B-specific proteins have a role in the coordinate regulation of this growth factor-growth factor receptor gene system that controls T cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoyos, B -- Ballard, D W -- Bohnlein, E -- Siekevitz, M -- Greene, W C -- A127053-01/PHS HHS/ -- New York, N.Y. -- Science. 1989 Apr 28;244(4903):457-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mount Sinai Medical Center, Department of Microbiology, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2497518" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line ; Cloning, Molecular ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; *Enhancer Elements, Genetic ; *Gene Expression Regulation ; Genes, Viral ; HIV-1/genetics ; HTLV-I Antigens/pharmacology ; Humans ; Immunoglobulin kappa-Chains/*genetics ; Interleukin-2/*genetics ; Molecular Weight ; Mutation ; Phytohemagglutinins/pharmacology ; Plasmids ; Promoter Regions, Genetic ; RNA, Messenger/biosynthesis ; T-Lymphocytes/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Trans-Activators ; Transcription Factors/pharmacology ; Transcription, Genetic ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Bacterial blight of soybean: regulation of a pathogen gene determining host cultivar specificity (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-09-22
    Description: Soybean cultivars resistant to Pseudomonas syringae pathovar glycinea (Psg), the causal agent of bacterial blight, exhibit a hypersensitive (necrosis) reaction (HR) to infection. Psg strains carrying the avrB gene elicit the HR in soybean cultivars carrying the resistance gene Rpg1. Psg expressing avrB at a high level and capable of eliciting the HR in the absence of de novo bacterial RNA synthesis have been obtained in in vitro culture. Nutritional signals and regions within the Psg hrp gene cluster, an approximately 20-kilobase genomic region also necessary for pathogenicity, control avrB transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huynh, T V -- Dahlbeck, D -- Staskawicz, B J -- New York, N.Y. -- Science. 1989 Sep 22;245(4924):1374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Pathology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2781284" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; DNA Mutational Analysis ; Gene Expression Regulation ; Genes, Bacterial ; *Plant Diseases ; Promoter Regions, Genetic ; Pseudomonas/*genetics/growth & development/pathogenicity ; Regulatory Sequences, Nucleic Acid ; Restriction Mapping ; Soybeans/*genetics/microbiology ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 94
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    Effect of antisense c-raf-1 on tumorigenicity and radiation sensitivity of a human squamous carcinoma (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-03-10
    Description: Antisense RNA-mediated inhibition of gene expression was used to investigate the biological function of the c-raf-1 gene in a radiation-resistant human squamous carcinoma cell line, SQ-20B. S1 nuclease protection assays revealed that transfection of full-length raf complementary DNA in the antisense orientation (AS) leads to a specific reduction (greater than tenfold) of steady-state levels of the endogenous c-raf-1 sense (S) transcript in SQ-20B cells. In nude mice, the malignant potential of SQ-20B cells transfected with raf (S) was significantly increased relative to that of SQ-20B cells transfected with raf (AS). SQ-20B cells containing transfected raf (S) maintained a radiation-resistant phenotype as compared to those cells harboring the AS version, which appeared to have enhanced radiation sensitivity. These data indicate that the reduced expression of endogenous c-raf-1 is sufficient to modulate the tumorigenicity and the radiation-resistant phenotype of SQ-20B cells, thus implicating c-raf-1 in a pathway important to the genesis of this type of cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasid, U -- Pfeifer, A -- Brennan, T -- Beckett, M -- Weichselbaum, R R -- Dritschilo, A -- Mark, G E -- New York, N.Y. -- Science. 1989 Mar 10;243(4896):1354-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Radiation Medicine, Vincent T. Lombardi Comprehensive Cancer Research Center, Georgetown University Medical Center, Washington 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2466340" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blotting, Southern ; Carcinoma, Squamous Cell/*genetics ; Cell Line ; Cell Survival/*radiation effects ; Clone Cells ; Dose-Response Relationship, Radiation ; *Gene Expression Regulation ; Humans ; Kinetics ; Mice ; Mice, Nude ; Neoplasm Transplantation ; Nucleic Acid Hybridization ; *Proto-Oncogenes ; RNA/*genetics ; RNA, Antisense ; RNA, Messenger/*antagonists & inhibitors ; Transcription, Genetic ; Transfection ; Transplantation, Heterologous ; Tumor Cells, Cultured/*radiation effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    cis-trans models for post-transcriptional gene regulation (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klausner, R D -- Harford, J B -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):870-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2683086" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Gene Expression Regulation ; *Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Protein Biosynthesis ; RNA, Messenger/genetics ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 96
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    Switch protein alters specificity of RNA polymerase containing a compartment-specific sigma factor (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-27
    Description: During sporulation in Bacillus subtilis, expression of developmental genes spoIVCB and cotD is induced in the mother cell compartment of the sporangium at morphological stages IV and V, respectively. A 27-kilodalton RNA polymerase sigma factor called sigma K (or sigma 27) has been found that causes weak transcription of spoIVCB and strong transcription of cotD. A 14-kD protein was also discovered that changes the specificity of sigma K-containing RNA polymerase, greatly stimulating spoIVCB transcription and markedly repressing cotD transcription. Both sigma K and the 14-kD protein are products of genes known to be required for expression of specific genes in the mother cell. Thus, sigma K directs gene expression in the mother cell and it is proposed that inactivation or sequestering of the 14-kD protein switches the temporal pattern of gene expression during the transition from stages IV to V of development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kroos, L -- Kunkel, B -- Losick, R -- GM18568/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Jan 27;243(4890):526-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2492118" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillus subtilis/*genetics/physiology ; Cloning, Molecular ; DNA-Directed RNA Polymerases/*genetics/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation ; Molecular Sequence Data ; Promoter Regions, Genetic ; Sigma Factor/*genetics/isolation & purification ; Spores, Bacterial/genetics ; Transcription Factors/*genetics ; Transcription, Genetic
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  • 97
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    S phase of the cell cycle (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-03
    Description: In each cell cycle the complex structure of the chromosome must be replicated accurately. In the last few years there have been major advances in understanding eukaryotic chromosome replication. Patterns of replication origins have been mapped accurately in yeast chromosomes. Cellular replication proteins have been identified by fractionating cell extracts that replicate viral DNA templates in vitro. Cell-free systems that initiate eukaryotic DNA replication in vitro have demonstrated the importance of complex nuclear architecture in the control of DNA replication. Although the events of S phase were relatively neglected for many years, knowledge of DNA replication is now advancing rapidly in step with other phases of the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laskey, R A -- Fairman, M P -- Blow, J J -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):609-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, England.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2683076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/physiology/ultrastructure ; Chromatin/physiology ; Chromosomes/physiology ; *DNA Replication ; *Interphase ; Models, Biological ; Transcription, Genetic
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  • 98
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    Repression of the IgH enhancer in teratocarcinoma cells associated with a novel octamer factor (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-27
    Description: Embryonal carcinoma (EC) cell lines are models for early cells in mouse embryogenesis. A 300-base pair fragment of the heavy chain enhancer was inactive in F9 EC cells, unlike in other nonlymphoid cells where it has significant activity. Alterations of the octamer motif increased enhancer activity. Nuclear extracts from F9 cells contained an octamer binding protein (NF-A3) that was unique to EC cells; the amount of NF-A3 decreased upon differentiation. It is proposed that NF-A3 represses specific regulatory sequences that contain the octamer motif. Thus, the same DNA sequence mediates either negative or positive transcriptional effects, depending on the cell type.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lenardo, M J -- Staudt, L -- Robbins, P -- Kuang, A -- Mulligan, R C -- Baltimore, D -- CA 01074/CA/NCI NIH HHS/ -- HD0063/HD/NICHD NIH HHS/ -- HL37569/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Jan 27;243(4890):544-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2536195" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bucladesine/pharmacology ; Cell Differentiation ; DNA/metabolism ; Embryonal Carcinoma Stem Cells ; *Enhancer Elements, Genetic ; Immunoglobulin Heavy Chains/*genetics ; Macromolecular Substances ; Mice ; Mutation ; Neoplastic Stem Cells/*metabolism ; RNA, Messenger/biosynthesis ; Regulatory Sequences, Nucleic Acid ; Repressor Proteins/genetics ; Transcription, Genetic ; Transfection ; Tretinoin/pharmacology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Selective amplification and cloning of four new members of the G protein-coupled receptor family (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-05
    Description: An approach based on the polymerase chain reaction has been devised to clone new members of the family of genes encoding guanosine triphosphate-binding protein (G protein)-coupled receptors. Degenerate primers corresponding to consensus sequences of the third and sixth transmembrane segments of available receptors were used to selectively amplify and clone members of this gene family from thyroid complementary DNA. Clones encoding three known receptors and four new putative receptors were obtained. Sequence comparisons established that the new genes belong to the G protein-coupled receptor family. Close structural similarity was observed between one of the putative receptors and the 5HT1a receptor. Two other molecules displayed common sequence characteristics, suggesting that they are members of a new subfamily of receptors with a very short nonglycosylated (extracellular) amino-terminal extension.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Libert, F -- Parmentier, M -- Lefort, A -- Dinsart, C -- Van Sande, J -- Maenhaut, C -- Simons, M J -- Dumont, J E -- Vassart, G -- New York, N.Y. -- Science. 1989 May 5;244(4904):569-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Recherche Interdisciplinaire, Faculte de Medecine, Universite Libre de Bruxelles, Campus Erasme, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2541503" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; DNA/genetics ; DNA-Directed DNA Polymerase ; GTP-Binding Proteins/*metabolism ; *Gene Amplification ; Humans ; Molecular Sequence Data ; Receptors, Adrenergic, alpha/genetics ; Receptors, Adrenergic, beta/genetics ; Receptors, Muscarinic/genetics ; Receptors, Neurokinin-2 ; Receptors, Neurotransmitter/*genetics ; Receptors, Serotonin/genetics ; Sequence Homology, Nucleic Acid ; Thyroid Gland/analysis ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-21
    Description: Quiescent T cells can be induced to express many genes by mitogen or antigen stimulation. The messenger RNAs of some of these genes undergo relatively rapid degradation compared to messenger RNAs from constitutively expressed genes. A T cell activation pathway that specifically regulates the stability of messenger RNAs for the lymphokines interleukin-2, interferon-gamma, tumor necrosis factor-alpha, and granulocyte-macrophage colony-stimulating factor is induced by stimulation of the CD28 surface molecule. This pathway does not directly affect the steady-state messenger RNA level, transcription, or messenger RNA half-life of other T cell activation genes, including c-myc, c-fos, IL-2 receptor, and the 4F2HC surface antigen. These data show that stimuli received at the cell surface can alter gene expression by inducing specific changes in messenger RNA degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lindstein, T -- June, C H -- Ledbetter, J A -- Stella, G -- Thompson, C B -- New York, N.Y. -- Science. 1989 Apr 21;244(4902):339-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2540528" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD28 ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/immunology ; Colony-Stimulating Factors/genetics ; Drug Stability ; Gene Expression Regulation ; Granulocyte-Macrophage Colony-Stimulating Factor ; Growth Substances/genetics ; Interferon-gamma/genetics ; Interleukin-2/genetics ; *Lymphocyte Activation ; Lymphokines/*genetics ; RNA, Messenger/genetics/*metabolism ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/*immunology ; Transcription, Genetic ; Tumor Necrosis Factor-alpha/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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