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  • Base Sequence  (59)
  • American Association for the Advancement of Science (AAAS)  (59)
  • American Institute of Physics (AIP)
  • Annual Reviews
  • 2005-2009  (26)
  • 1990-1994
  • 1980-1984  (33)
  • 1950-1954
  • 2007  (26)
  • 1983  (33)
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  • American Association for the Advancement of Science (AAAS)  (59)
  • American Institute of Physics (AIP)
  • Annual Reviews
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  • 2005-2009  (26)
  • 1990-1994
  • 1980-1984  (33)
  • 1950-1954
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  • 1
    Publication Date: 2007-10-27
    Description: We report the cloning of Style2.1, the major quantitative trait locus responsible for a key floral attribute (style length) associated with the evolution of self-pollination in cultivated tomatoes. The gene encodes a putative transcription factor that regulates cell elongation in developing styles. The transition from cross-pollination to self-pollination was accompanied, not by a change in the STYLE2.1 protein, but rather by a mutation in the Style2.1 promoter that results in a down-regulation of Style2.1 expression during flower development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Kai-Yi -- Cong, Bin -- Wing, Rod -- Vrebalov, Julia -- Tanksley, Steven D -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):643-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Breeding and Genetics, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962563" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Chromosome Mapping ; Cloning, Molecular ; Crosses, Genetic ; Down-Regulation ; Flowers/*anatomy & histology/genetics/growth & development ; Genes, Plant ; Genotype ; Helix-Loop-Helix Motifs ; Lycopersicon esculentum/anatomy & histology/*genetics/*physiology ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/metabolism ; Pollen/physiology ; Promoter Regions, Genetic ; Quantitative Trait Loci ; Reproduction ; Sequence Deletion ; Transcription Factors/chemistry/*genetics/metabolism ; Transformation, Genetic
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  • 2
    Publication Date: 2007-04-14
    Description: A systematic fluorescence in situ hybridization comparison of macaque and human synteny organization disclosed five additional macaque evolutionary new centromeres (ENCs) for a total of nine ENCs. To understand the dynamics of ENC formation and progression, we compared the ENC of macaque chromosome 4 with the human orthologous region, at 6q24.3, that conserves the ancestral genomic organization. A 250-kilobase segment was extensively duplicated around the macaque centromere. These duplications were strictly intrachromosomal. Our results suggest that novel centromeres may trigger only local duplication activity and that the absence of genes in the seeding region may have been important in ENC maintenance and progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ventura, Mario -- Antonacci, Francesca -- Cardone, Maria Francesca -- Stanyon, Roscoe -- D'Addabbo, Pietro -- Cellamare, Angelo -- Sprague, L James -- Eichler, Evan E -- Archidiacono, Nicoletta -- Rocchi, Mariano -- GM58815/GM/NIGMS NIH HHS/ -- HG002385/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Microbiology, University of Bari, 70126 Bari, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431171" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Centromere ; Chromosomes, Human, Pair 6 ; Dna ; *Evolution, Molecular ; Gene Duplication ; Humans ; Macaca mulatta/*genetics ; Molecular Sequence Data ; Sequence Tagged Sites ; Synteny
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  • 3
    Publication Date: 2007-10-20
    Description: A computational analysis of the nuclear genome of a red alga, Cyanidioschyzon merolae, identified 11 transfer RNA (tRNA) genes in which the 3' half of the tRNA lies upstream of the 5' half in the genome. We verified that these genes are expressed and produce mature tRNAs that are aminoacylated. Analysis of tRNA-processing intermediates for these genes indicates an unusual processing pathway in which the termini of the tRNA precursor are ligated, resulting in formation of a characteristic circular RNA intermediate that is then processed at the acceptor stem to generate the correct termini.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soma, Akiko -- Onodera, Akinori -- Sugahara, Junichi -- Kanai, Akio -- Yachie, Nozomu -- Tomita, Masaru -- Kawamura, Fujio -- Sekine, Yasuhiko -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):450-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Life Science, College of Science, Rikkyo (St. Paul's) University, Toshima, Tokyo 171-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947580" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Algal/chemistry/genetics ; *Genes ; Methionine-tRNA Ligase/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/chemistry/genetics/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Algal/*genetics/metabolism ; RNA, Transfer/*genetics/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Rhodophyta/*genetics/metabolism ; Transcription, Genetic
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  • 4
    Publication Date: 2007-07-14
    Description: The temporal and spatial regulation of gene expression in mammalian development is linked to the establishment of functional chromatin domains. Here, we report that tissue-specific transcription of a retrotransposon repeat in the murine growth hormone locus is required for gene activation. This repeat serves as a boundary to block the influence of repressive chromatin modifications. The repeat element is able to generate short, overlapping Pol II-and Pol III-driven transcripts, both of which are necessary and sufficient to enable a restructuring of the regulated locus into nuclear compartments. These data suggest that transcription of interspersed repetitive sequences may represent a developmental strategy for the establishment of functionally distinct domains within the mammalian genome to control gene activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lunyak, Victoria V -- Prefontaine, Gratien G -- Nunez, Esperanza -- Cramer, Thorsten -- Ju, Bong-Gun -- Ohgi, Kenneth A -- Hutt, Kasey -- Roy, Rosa -- Garcia-Diaz, Angel -- Zhu, Xiaoyan -- Yung, Yun -- Montoliu, Lluis -- Glass, Christopher K -- Rosenfeld, Michael G -- New York, N.Y. -- Science. 2007 Jul 13;317(5835):248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, School of Medicine, University of California, San Diego, 9500 Gilman Drive, Room 345, La Jolla, CA 92093-0648, USA. vlunyak@uscd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17626886" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromatin Immunoprecipitation ; DNA Polymerase II/metabolism ; DNA Polymerase III/metabolism ; *Gene Expression Regulation, Developmental ; Growth Hormone/*genetics ; Histones/metabolism ; *Insulator Elements ; Methylation ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Organogenesis ; Pituitary Gland/*embryology/metabolism ; *Short Interspersed Nucleotide Elements ; *Transcription, Genetic ; Transcriptional Activation
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  • 5
    Publication Date: 2007-06-30
    Description: HIV-1 integrates into the host chromosome and persists as a provirus flanked by long terminal repeats (LTRs). To date, treatment regimens primarily target the virus enzymes or virus-cell fusion, but not the integrated provirus. We report here the substrate-linked protein evolution of a tailored recombinase that recognizes an asymmetric sequence within an HIV-1 LTR. This evolved recombinase efficiently excised integrated HIV proviral DNA from the genome of infected cells. Although a long way from use in the clinic, we speculate that this type of technology might be adapted in future antiretroviral therapies, among other possible uses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sarkar, Indrani -- Hauber, Ilona -- Hauber, Joachim -- Buchholz, Frank -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1912-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, D-01307 Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600219" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Shuffling ; DNA, Viral/*metabolism ; *Directed Molecular Evolution ; Escherichia coli/genetics ; Gene Library ; Genome, Human ; *HIV Long Terminal Repeat ; HIV-1/*metabolism ; HeLa Cells ; Humans ; Integrases/*genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Proviruses/metabolism ; Recombination, Genetic ; *Virus Integration
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  • 6
    Publication Date: 2007-01-16
    Description: A major goal of systems biology is to predict the function of biological networks. Although network topologies have been successfully determined in many cases, the quantitative parameters governing these networks generally have not. Measuring affinities of molecular interactions in high-throughput format remains problematic, especially for transient and low-affinity interactions. We describe a high-throughput microfluidic platform that measures such properties on the basis of mechanical trapping of molecular interactions. With this platform we characterized DNA binding energy landscapes for four eukaryotic transcription factors; these landscapes were used to test basic assumptions about transcription factor binding and to predict their in vivo function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maerkl, Sebastian J -- Quake, Stephen R -- New York, N.Y. -- Science. 2007 Jan 12;315(5809):233-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry and Molecular Biophysics Option, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17218526" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Basic Helix-Loop-Helix Transcription Factors/*metabolism ; Computational Biology ; Computer Simulation ; DNA/*metabolism ; DNA, Fungal/genetics/metabolism ; DNA-Binding Proteins/metabolism ; E-Box Elements ; Gene Expression Regulation, Fungal ; Helix-Loop-Helix Motifs ; Humans ; *Microfluidic Analytical Techniques ; Oligonucleotide Array Sequence Analysis ; Protein Binding ; Protein Isoforms/metabolism ; Regulatory Sequences, Nucleic Acid ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; *Systems Biology ; Templates, Genetic ; Thermodynamics ; Transcription Factors/metabolism
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  • 7
    Publication Date: 2007-11-03
    Description: Increasingly complex networks of small RNAs act through RNA-interference (RNAi) pathways to regulate gene expression, to mediate antiviral responses, to organize chromosomal domains, and to restrain the spread of selfish genetic elements. Historically, RNAi has been defined as a response to double-stranded RNA. However, some small RNA species may not arise from double-stranded RNA precursors. Yet, like microRNAs and small interfering RNAs, such species guide Argonaute proteins to silencing targets through complementary base-pairing. Silencing can be achieved by corecruitment of accessory factors or through the activity of Argonaute itself, which often has endonucleolytic activity. As a specific and adaptive regulatory system, RNAi is used throughout eukarya, which indicates a long evolutionary history. A likely function of RNAi throughout that history is to protect the genome from both pathogenic and parasitic invaders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aravin, Alexei A -- Hannon, Gregory J -- Brennecke, Julius -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):761-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Watson School of Biological Sciences, Howard Hughes Medical Institute, 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/17975059" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Biological ; Animals ; Argonaute Proteins ; Base Sequence ; *DNA Transposable Elements ; Drosophila Proteins ; Evolution, Molecular ; Gene Silencing ; Molecular Sequence Data ; Proteins/genetics/physiology ; *RNA, Small Interfering ; RNA-Binding Proteins/genetics/*physiology ; RNA-Induced Silencing Complex
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-10-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):190-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932267" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Classification/methods ; Computational Biology ; DNA Probes ; DNA, Chloroplast/*genetics ; DNA, Intergenic/*genetics ; Databases, Nucleic Acid ; Genes, Plant ; Plants/*classification/*genetics ; Plants, Medicinal/classification/genetics ; Sequence Analysis, DNA ; Trees/classification/genetics
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  • 9
    Publication Date: 2007-01-06
    Description: MicroRNAs (miRNAs) negatively regulate partially complementary target messenger RNAs. Target selection in animals is dictated primarily by sequences at the miRNA 5' end. We demonstrated that despite their small size, specific miRNAs contain additional sequence elements that control their posttranscriptional behavior, including their subcellular localization. We showed that human miR-29b, in contrast to other studied animal miRNAs, is predominantly localized to the nucleus. The distinctive hexanucleotide terminal motif of miR-29b acts as a transferable nuclear localization element that directs nuclear enrichment of miRNAs or small interfering RNAs to which it is attached. Our results indicate that miRNAs sharing common 5' sequences, considered to be largely redundant, might have distinct functions because of the influence of cis-acting regulatory motifs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, Hun-Way -- Wentzel, Erik A -- Mendell, Joshua T -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Human Genetics and Molecular Biology, McKusick-Nathans Institute of Genetic Medicine, 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/17204650" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Apoptosis ; Base Sequence ; Cell Nucleus/*metabolism ; HeLa Cells ; Humans ; Mice ; MicroRNAs/*chemistry/*metabolism ; Mitosis ; Mutation ; NIH 3T3 Cells ; Oligoribonucleotides/chemistry/*metabolism ; RNA Processing, Post-Transcriptional ; RNA Stability ; RNA, Small Interfering ; Reverse Transcriptase Polymerase Chain Reaction ; Ribonuclease III/metabolism ; Transcription, Genetic
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  • 10
    Publication Date: 2007-06-02
    Description: Sponges (phylum Porifera) were prolific reef-building organisms during the Paleozoic and Mesozoic approximately 542 to 65 million years ago. These ancient animals inherited components of the first multicellular skeletogenic toolkit from the last common ancestor of the Metazoa. Using a paleogenomics approach, including gene- and protein-expression techniques and phylogenetic reconstruction, we show that a molecular component of this toolkit was the precursor to the alpha-carbonic anhydrases (alpha-CAs), a gene family used by extant animals in a variety of fundamental physiological processes. We used the coralline demosponge Astrosclera willeyana, a "living fossil" that has survived from the Mesozoic, to provide insight into the evolution of the ability to biocalcify, and show that the alpha-CA family expanded from a single ancestral gene through several independent gene-duplication events in sponges and eumetazoans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jackson, Daniel J -- Macis, Luciana -- Reitner, Joachim -- Degnan, Bernard M -- Worheide, Gert -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1893-5. Epub 2007 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geoscience Centre Gottingen, Department of Geobiology, Goldschmidtstrasse 3, D-37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540861" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Bicarbonates/metabolism ; *Calcification, Physiologic ; Calcium Carbonate/analysis/metabolism ; Carbonic Anhydrases/chemistry/*genetics/*metabolism ; Computational Biology ; Evolution, Molecular ; Gene Duplication ; Genes ; Genomics ; Molecular Sequence Data ; Porifera/anatomy & histology/enzymology/*genetics/*physiology ; Recombinant Proteins/chemistry/metabolism
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  • 11
    Publication Date: 2007-07-21
    Description: The genomes of individuals from the same species vary in sequence as a result of different evolutionary processes. To examine the patterns of, and the forces shaping, sequence variation in Arabidopsis thaliana, we performed high-density array resequencing of 20 diverse strains (accessions). More than 1 million nonredundant single-nucleotide polymorphisms (SNPs) were identified at moderate false discovery rates (FDRs), and approximately 4% of the genome was identified as being highly dissimilar or deleted relative to the reference genome sequence. Patterns of polymorphism are highly nonrandom among gene families, with genes mediating interaction with the biotic environment having exceptional polymorphism levels. At the chromosomal scale, regional variation in polymorphism was readily apparent. A scan for recent selective sweeps revealed several candidate regions, including a notable example in which almost all variation was removed in a 500-kilobase window. Analyzing the polymorphisms we describe in larger sets of accessions will enable a detailed understanding of forces shaping population-wide sequence variation in A. thaliana.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, Richard M -- Schweikert, Gabriele -- Toomajian, Christopher -- Ossowski, Stephan -- Zeller, Georg -- Shinn, Paul -- Warthmann, Norman -- Hu, Tina T -- Fu, Glenn -- Hinds, David A -- Chen, Huaming -- Frazer, Kelly A -- Huson, Daniel H -- Scholkopf, Bernhard -- Nordborg, Magnus -- Ratsch, Gunnar -- Ecker, Joseph R -- Weigel, Detlef -- New York, N.Y. -- Science. 2007 Jul 20;317(5836):338-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17641193" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Arabidopsis/*genetics ; Base Sequence ; Chromosomes, Plant/genetics ; Computational Biology ; Gene Frequency ; Genes, Plant ; *Genetic Variation ; *Genome, Plant ; Molecular Sequence Data ; *Polymorphism, Genetic ; *Polymorphism, Single Nucleotide ; Selection, Genetic ; Sequence Analysis, DNA
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  • 12
    Publication Date: 2007-01-20
    Description: Cysteine (Cys) residues often play critical roles in proteins; however, identification of their specific functions has been limited to case-by-case experimental approaches. We developed a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases. This method is independent of protein family, structure, and taxon. We used it to selectively detect the majority of known proteins with redox-active Cys and to make additional predictions, one of which was verified. Rapid accumulation of sequence information from genomic and metagenomic projects should allow detection of many additional oxidoreductase families as well as identification of redox-active Cys in these proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fomenko, Dmitri E -- Xing, Weibing -- Adair, Blakely M -- Thomas, David J -- Gladyshev, Vadim N -- AG021518/AG/NIA NIH HHS/ -- GM061603/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):387-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17234949" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Archaeal Proteins/chemistry ; Bacterial Proteins/chemistry ; Base Sequence ; Catalysis ; Computational Biology ; Cysteine/analysis/*chemistry ; *Databases, Nucleic Acid ; *Databases, Protein ; Enzymes/*chemistry ; Eukaryotic Cells ; Evolution, Molecular ; Methyltransferases/chemistry ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/chemistry ; Proteins/*chemistry ; Selenocysteine/chemistry ; Selenoproteins/*chemistry
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  • 13
    Publication Date: 2007-06-26
    Description: Primate genomes contain a large number of endogenous retroviruses and encode evolutionarily dynamic proteins that provide intrinsic immunity to retroviral infections. We report here the resurrection of the core protein of a 4-million-year-old endogenous virus from the chimpanzee genome and show that the human variant of the intrinsic immune protein TRIM5alpha can actively prevent infection by this virus. However, we suggest that selective changes that have occurred in the human lineage during the acquisition of resistance to this virus, and perhaps similar viruses, may have left our species more susceptible to infection by human immunodeficiency virus type 1 (HIV-1).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Shari M -- Malik, Harmit S -- Emerman, Michael -- New York, N.Y. -- Science. 2007 Jun 22;316(5832):1756-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular and Cellular Biology Program, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17588933" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Carrier Proteins/genetics/*physiology ; Cats ; Cell Line ; Dna ; Disease Susceptibility ; Endogenous Retroviruses/genetics/*physiology ; Evolution, Molecular ; Gorilla gorilla ; HIV Infections/genetics/immunology ; Hiv-1 ; Humans ; Immunity, Innate/genetics ; Macaca mulatta ; Molecular Sequence Data ; Pan troglodytes/genetics/virology ; Retroviridae Infections/genetics/immunology
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  • 14
    Publication Date: 2007-02-27
    Description: Primary transcripts of certain microRNA (miRNA) genes are subject to RNA editing that converts adenosine to inosine. However, the importance of miRNA editing remains largely undetermined. Here we report that tissue-specific adenosine-to-inosine editing of miR-376 cluster transcripts leads to predominant expression of edited miR-376 isoform RNAs. One highly edited site is positioned in the middle of the 5'-proximal half "seed" region critical for the hybridization of miRNAs to targets. We provide evidence that the edited miR-376 RNA silences specifically a different set of genes. Repression of phosphoribosyl pyrophosphate synthetase 1, a target of the edited miR-376 RNA and an enzyme involved in the uric-acid synthesis pathway, contributes to tight and tissue-specific regulation of uric-acid levels, revealing a previously unknown role for RNA editing in miRNA-mediated gene silencing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2953418/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2953418/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawahara, Yukio -- Zinshteyn, Boris -- Sethupathy, Praveen -- Iizasa, Hisashi -- Hatzigeorgiou, Artemis G -- Nishikura, Kazuko -- P01 CA072765/CA/NCI NIH HHS/ -- P01 CA072765-050002/CA/NCI NIH HHS/ -- R01 GM040536/GM/NIGMS NIH HHS/ -- R01 GM040536-16/GM/NIGMS NIH HHS/ -- R01 HL070045/HL/NHLBI NIH HHS/ -- R01 HL070045-04/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 23;315(5815):1137-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA. ykawahara@wistar.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17322061" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions ; Adenosine/*metabolism ; Adenosine Deaminase/genetics/metabolism ; Animals ; Base Sequence ; Brain/metabolism ; HeLa Cells ; Humans ; Inosine/*metabolism ; Liver/metabolism ; Mice ; MicroRNAs/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Organ Specificity ; Protein-Serine-Threonine Kinases/genetics/metabolism ; *RNA Editing ; *RNA Interference ; RNA-Binding Proteins ; Ribose-Phosphate Pyrophosphokinase/genetics/metabolism ; Uric Acid/metabolism
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  • 15
    Publication Date: 2007-08-11
    Description: Characterization of interspecies differences in gene regulation is crucial for understanding the molecular basis of both phenotypic diversity and evolution. By means of chromatin immunoprecipitation and DNA microarray analysis, the divergence in the binding sites of the pseudohyphal regulators Ste12 and Tec1 was determined in the yeasts Saccharomyces cerevisiae, S. mikatae, and S. bayanus under pseudohyphal conditions. We have shown that most of these sites have diverged across these species, far exceeding the interspecies variation in orthologous genes. A group of Ste12 targets was shown to be bound only in S. mikatae and S. bayanus under pseudohyphal conditions. Many of these genes are targets of Ste12 during mating in S. cerevisiae, indicating that specialization between the two pathways has occurred in this species. Transcription factor binding sites have therefore diverged substantially faster than ortholog content. Thus, gene regulation resulting from transcription factor binding is likely to be a major cause of divergence between related species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Borneman, Anthony R -- Gianoulis, Tara A -- Zhang, Zhengdong D -- Yu, Haiyuan -- Rozowsky, Joel -- Seringhaus, Michael R -- Wang, Lu Yong -- Gerstein, Mark -- Snyder, Michael -- New York, N.Y. -- Science. 2007 Aug 10;317(5839):815-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular and Developmental 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/17690298" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Candida albicans/genetics/growth & development/metabolism ; Chromatin Immunoprecipitation ; DNA-Binding Proteins/genetics/metabolism ; *Evolution, Molecular ; Fungal Proteins/genetics/*metabolism ; Gene Expression Regulation, Fungal ; Gene Regulatory Networks ; Genes, Fungal ; Oligonucleotide Array Sequence Analysis ; *Regulatory Sequences, Nucleic Acid ; Saccharomyces/*genetics/growth & development/metabolism ; Saccharomyces cerevisiae/*genetics/growth & development/metabolism ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Transcription Factors/genetics/*metabolism
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  • 16
    Publication Date: 2007-10-20
    Description: Hundreds of species of reef-building corals spawn synchronously over a few nights each year, and moonlight regulates this spawning event. However, the molecular elements underpinning the detection of moonlight remain unknown. Here we report the presence of an ancient family of blue-light-sensing photoreceptors, cryptochromes, in the reef-building coral Acropora millepora. In addition to being cryptochrome genes from one of the earliest-diverging eumetazoan phyla, cry1 and cry2 were expressed preferentially in light. Consistent with potential roles in the synchronization of fundamentally important behaviors such as mass spawning, cry2 expression increased on full moon nights versus new moon nights. Our results demonstrate phylogenetically broad roles of these ancient circadian clock-related molecules in the animal kingdom.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, O -- Appelbaum, L -- Leggat, W -- Gothlif, Y -- Hayward, D C -- Miller, D J -- Hoegh-Guldberg, O -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):467-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Marine Studies, University of Queensland, St. Lucia 4072 QLD, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947585" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/*genetics/*metabolism ; Base Sequence ; Circadian Rhythm ; Cryptochromes ; Flavoproteins/analysis/*genetics/*metabolism ; Gene Expression Regulation ; *Light ; Molecular Sequence Data ; Moon
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  • 17
    Publication Date: 2007-06-30
    Description: Circadian and other natural clock-like endogenous rhythms may have evolved to anticipate regular temporal changes in the environment. We report that a mutation in the circadian clock gene timeless in Drosophila melanogaster has arisen and spread by natural selection relatively recently in Europe. We found that, when introduced into different genetic backgrounds, natural and artificial alleles of the timeless gene affect the incidence of diapause in response to changes in light and temperature. The natural mutant allele alters an important life history trait that may enhance the fly's adaptation to seasonal conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tauber, Eran -- Zordan, Mauro -- Sandrelli, Federica -- Pegoraro, Mirko -- Osterwalder, Nicolo -- Breda, Carlo -- Daga, Andrea -- Selmin, Alessandro -- Monger, Karen -- Benna, Clara -- Rosato, Ezio -- Kyriacou, Charalambos P -- Costa, Rodolfo -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1895-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Leicester, Leicester LE1 7RH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600215" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Circadian Rhythm/genetics ; Drosophila Proteins/*genetics/physiology ; Drosophila melanogaster/*genetics/*physiology ; Europe ; Evolution, Molecular ; Female ; Geography ; Haplotypes ; Molecular Sequence Data ; Mutation ; *Photoperiod ; Phylogeny ; Polymorphism, Genetic ; Protein Isoforms/genetics/physiology ; Reproduction ; *Seasons ; *Selection, Genetic ; Temperature ; Transformation, Genetic
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  • 18
    Publication Date: 2007-10-27
    Description: Plant disease resistance (R) proteins recognize matching pathogen avirulence proteins. Alleles of the pepper R gene Bs3 mediate recognition of the Xanthomonas campestris pv. vesicatoria (Xcv) type III effector protein AvrBs3 and its deletion derivative AvrBs3Deltarep16. Pepper Bs3 and its allelic variant Bs3-E encode flavin monooxygenases with a previously unknown structure and are transcriptionally activated by the Xcv effector proteins AvrBs3 and AvrBs3Deltarep16, respectively. We found that recognition specificity resides in the Bs3 and Bs3-E promoters and is determined by binding of AvrBs3 or AvrBs3Deltarep16 to a defined promoter region. Our data suggest a recognition mechanism in which the Avr protein binds and activates the promoter of the cognate R gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Romer, Patrick -- Hahn, Simone -- Jordan, Tina -- Strauss, Tina -- Bonas, Ulla -- Lahaye, Thomas -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):645-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biology, Department of Genetics, Martin-Luther-University Halle-Wittenberg, D-06099 Halle (Saale), Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962564" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Bacterial Proteins/genetics/*metabolism ; Base Sequence ; Capsicum/*genetics/*microbiology ; Chromosomes, Artificial, Bacterial ; Gene Expression Regulation, Plant ; *Genes, Plant ; Mixed Function Oxygenases/chemistry/*genetics ; Molecular Sequence Data ; Plant Diseases/immunology/microbiology ; Plant Leaves/genetics/metabolism ; Plant Proteins/chemistry/genetics ; *Promoter Regions, Genetic ; Tobacco/genetics ; Transcription, Genetic ; Transformation, Genetic ; Xanthomonas campestris/genetics/metabolism/*pathogenicity
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  • 19
    Publication Date: 2007-10-20
    Description: Nonhomologous end joining (NHEJ) is a critical DNA double-strand break (DSB) repair pathway required to maintain genome stability. Many prokaryotes possess a minimalist NHEJ apparatus required to repair DSBs during stationary phase, composed of two conserved core proteins, Ku and ligase D (LigD). The crystal structure of Mycobacterium tuberculosis polymerase domain of LigD mediating the synapsis of two noncomplementary DNA ends revealed a variety of interactions, including microhomology base pairing, mismatched and flipped-out bases, and 3' termini forming hairpin-like ends. Biochemical and biophysical studies confirmed that polymerase-induced end synapsis also occurs in solution. We propose that this DNA synaptic structure reflects an intermediate bridging stage of the NHEJ process, before end processing and ligation, with both the polymerase and the DNA sequence playing pivotal roles in determining the sequential order of synapsis and remodeling before end joining.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brissett, Nigel C -- Pitcher, Robert S -- Juarez, Raquel -- Picher, Angel J -- Green, Andrew J -- Dafforn, Timothy R -- Fox, Gavin C -- Blanco, Luis -- Doherty, Aidan J -- BB/D522746/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G120/738/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):456-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947582" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Crystallography, X-Ray ; DNA Ligases/*chemistry/genetics/metabolism ; *DNA Repair ; DNA, Bacterial/*chemistry/metabolism ; Dimerization ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Mycobacterium tuberculosis/*chemistry/enzymology/genetics/metabolism ; Protein Conformation ; Protein Structure, Tertiary
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  • 20
    Publication Date: 2007-12-01
    Description: Molecular patterns in pathogenic RNAs can be recognized by the innate immune system, and a component of this response is the interferon-induced enzyme RNA-activated protein kinase (PKR). The major activators of PKR have been proposed to be long double-stranded RNAs. We report that RNAs with very limited secondary structures activate PKR in a 5'-triphosphate-dependent fashion in vitro and in vivo. Activation of PKR by 5'-triphosphate RNA is independent of RIG-I and is enhanced by treatment with type 1 interferon (IFN-alpha). Surveillance of molecular features at the 5' end of transcripts by PKR presents a means of allowing pathogenic RNA to be distinguished from self-RNA. The evidence presented here suggests that this form of RNA-based discrimination may be a critical step in mounting an early immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nallagatla, Subba Rao -- Hwang, Jungwook -- Toroney, Rebecca -- Zheng, Xiaofeng -- Cameron, Craig E -- Bevilacqua, Philip C -- GM58709/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1455-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048689" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line, Tumor ; Cercopithecus aethiops ; DEAD-box RNA Helicases/metabolism ; Enzyme Activation ; Eukaryotic Initiation Factor-2/metabolism ; Humans ; Immunity, Innate ; Interferon-alpha/immunology/metabolism ; Interferon-beta/metabolism ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Phosphoric Monoester Hydrolases/metabolism ; Polyphosphates/metabolism ; RNA/chemistry/genetics/*metabolism ; RNA, Double-Stranded/chemistry/genetics/*metabolism ; Transfection ; Vero Cells ; eIF-2 Kinase/*metabolism
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  • 21
    Publication Date: 2007-12-01
    Description: Both limiting and toxic soil concentrations of the essential micronutrient boron represent major limitations to crop production worldwide. We identified Bot1, a BOR1 ortholog, as the gene responsible for the superior boron-toxicity tolerance of the Algerian barley landrace Sahara 3771 (Sahara). Bot1 was located at the tolerance locus by high-resolution mapping. Compared to intolerant genotypes, Sahara contains about four times as many Bot1 gene copies, produces substantially more Bot1 transcript, and encodes a Bot1 protein with a higher capacity to provide tolerance in yeast. Bot1 transcript levels identified in barley tissues are consistent with a role in limiting the net entry of boron into the root and in the disposal of boron from leaves via hydathode guttation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sutton, Tim -- Baumann, Ute -- Hayes, Julie -- Collins, Nicholas C -- Shi, Bu-Jun -- Schnurbusch, Thorsten -- Hay, Alison -- Mayo, Gwenda -- Pallotta, Margaret -- Tester, Mark -- Langridge, Peter -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1446-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Australian Centre for Plant Functional Genomics, School of Agriculture, Food and Wine, University of Adelaide, Waite Campus, Private Mail Bag 1, Glen Osmond, South Australia 5064, Australia. tim.sutton@acpfg.com.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048688" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Transport ; Boron/metabolism/*toxicity ; Boron Compounds/*metabolism/*toxicity ; Chromosome Mapping ; *Genes, Plant ; Hordeum/*drug effects/*genetics/metabolism ; Membrane Transport Proteins/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Plant Lectins/genetics/metabolism ; Plant Proteins/chemistry/genetics/metabolism ; Plant Roots/genetics/metabolism ; Quantitative Trait Loci ; Saccharomyces cerevisiae/genetics/growth & development/metabolism ; Transcription, Genetic
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  • 22
    Publication Date: 2007-05-19
    Description: We present a draft sequence of the genome of Aedes aegypti, the primary vector for yellow fever and dengue fever, which at approximately 1376 million base pairs is about 5 times the size of the genome of the malaria vector Anopheles gambiae. Nearly 50% of the Ae. aegypti genome consists of transposable elements. These contribute to a factor of approximately 4 to 6 increase in average gene length and in sizes of intergenic regions relative to An. gambiae and Drosophila melanogaster. Nonetheless, chromosomal synteny is generally maintained among all three insects, although conservation of orthologous gene order is higher (by a factor of approximately 2) between the mosquito species than between either of them and the fruit fly. An increase in genes encoding odorant binding, cytochrome P450, and cuticle domains relative to An. gambiae suggests that members of these protein families underpin some of the biological differences between the two mosquito species.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2868357/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2868357/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nene, Vishvanath -- Wortman, Jennifer R -- Lawson, Daniel -- Haas, Brian -- Kodira, Chinnappa -- Tu, Zhijian Jake -- Loftus, Brendan -- Xi, Zhiyong -- Megy, Karyn -- Grabherr, Manfred -- Ren, Quinghu -- Zdobnov, Evgeny M -- Lobo, Neil F -- Campbell, Kathryn S -- Brown, Susan E -- Bonaldo, Maria F -- Zhu, Jingsong -- Sinkins, Steven P -- Hogenkamp, David G -- Amedeo, Paolo -- Arensburger, Peter -- Atkinson, Peter W -- Bidwell, Shelby -- Biedler, Jim -- Birney, Ewan -- Bruggner, Robert V -- Costas, Javier -- Coy, Monique R -- Crabtree, Jonathan -- Crawford, Matt -- Debruyn, Becky -- Decaprio, David -- Eiglmeier, Karin -- Eisenstadt, Eric -- El-Dorry, Hamza -- Gelbart, William M -- Gomes, Suely L -- Hammond, Martin -- Hannick, Linda I -- Hogan, James R -- Holmes, Michael H -- Jaffe, David -- Johnston, J Spencer -- Kennedy, Ryan C -- Koo, Hean -- Kravitz, Saul -- Kriventseva, Evgenia V -- Kulp, David -- Labutti, Kurt -- Lee, Eduardo -- Li, Song -- Lovin, Diane D -- Mao, Chunhong -- Mauceli, Evan -- Menck, Carlos F M -- Miller, Jason R -- Montgomery, Philip -- Mori, Akio -- Nascimento, Ana L -- Naveira, Horacio F -- Nusbaum, Chad -- O'leary, Sinead -- Orvis, Joshua -- Pertea, Mihaela -- Quesneville, Hadi -- Reidenbach, Kyanne R -- Rogers, Yu-Hui -- Roth, Charles W -- Schneider, Jennifer R -- Schatz, Michael -- Shumway, Martin -- Stanke, Mario -- Stinson, Eric O -- Tubio, Jose M C -- Vanzee, Janice P -- Verjovski-Almeida, Sergio -- Werner, Doreen -- White, Owen -- Wyder, Stefan -- Zeng, Qiandong -- Zhao, Qi -- Zhao, Yongmei -- Hill, Catherine A -- Raikhel, Alexander S -- Soares, Marcelo B -- Knudson, Dennis L -- Lee, Norman H -- Galagan, James -- Salzberg, Steven L -- Paulsen, Ian T -- Dimopoulos, George -- Collins, Frank H -- Birren, Bruce -- Fraser-Liggett, Claire M -- Severson, David W -- 079059/Wellcome Trust/United Kingdom -- 5 R01 AI61576-2/AI/NIAID NIH HHS/ -- R01 AI059492/AI/NIAID NIH HHS/ -- R01 LM006845/LM/NLM NIH HHS/ -- R01 LM006845-08/LM/NLM NIH HHS/ -- R37 AI024716/AI/NIAID NIH HHS/ -- UO1 AI50936/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Jun 22;316(5832):1718-23. Epub 2007 May 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, 9712 Medical Center Drive, Rockville, MD 20850, USA. nene@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510324" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/*genetics/metabolism ; Animals ; Anopheles gambiae/genetics/metabolism ; Arboviruses ; Base Sequence ; DNA Transposable Elements ; Dengue/prevention & control/transmission ; Drosophila melanogaster/genetics ; Female ; Genes, Insect ; *Genome, Insect ; Humans ; Insect Proteins/genetics ; Insect Vectors/*genetics/metabolism ; Male ; Membrane Transport Proteins/genetics ; Molecular Sequence Data ; Multigene Family ; Protein Structure, Tertiary/genetics ; Sequence Analysis, DNA ; Sex Characteristics ; Sex Determination Processes ; Species Specificity ; Synteny ; Transcription, Genetic ; Yellow Fever/prevention & control/transmission
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  • 23
    Publication Date: 2007-01-27
    Description: A mutualistic association between a fungal endophyte and a tropical panic grass allows both organisms to grow at high soil temperatures. We characterized a virus from this fungus that is involved in the mutualistic interaction. Fungal isolates cured of the virus are unable to confer heat tolerance, but heat tolerance is restored after the virus is reintroduced. The virus-infected fungus confers heat tolerance not only to its native monocot host but also to a eudicot host, which suggests that the underlying mechanism involves pathways conserved between these two groups of plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marquez, Luis M -- Redman, Regina S -- Rodriguez, Russell J -- Roossinck, Marilyn J -- New York, N.Y. -- Science. 2007 Jan 26;315(5811):513-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Division, Samuel Roberts Noble Foundation, Post Office Box 2180, Ardmore, OK 73402, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255511" target="_blank"〉PubMed〈/a〉
    Keywords: Ascomycota/growth & development/*physiology/*virology ; Base Sequence ; Hot Temperature ; Lycopersicon esculentum/microbiology/physiology ; Molecular Sequence Data ; Open Reading Frames ; Plant Leaves/metabolism ; Poaceae/growth & development/*microbiology/*physiology ; RNA Viruses/classification/genetics/isolation & purification/*physiology ; RNA, Double-Stranded/genetics/metabolism ; RNA, Viral/genetics/metabolism ; Reactive Oxygen Species/metabolism ; *Symbiosis
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  • 24
    Publication Date: 2007-09-01
    Description: Somatic hypermutation (SHM) is a major means by which diversity is achieved in antibody genes, and it is initiated by the deamination of cytosines to uracils in DNA by activation-induced deaminase (AID). However, the process that leads from these initiating deamination events to mutations at other residues remains poorly understood. We demonstrate that a single cytosine on the top (nontemplate) strand is sufficient to recruit AID and lead to mutations of upstream and downstream A/T residues. In contrast, the targeting of cytosines on the bottom strand by AID does not lead to substantial mutation of neighboring residues. This strand asymmetry is eliminated in mice deficient in mismatch repair, indicating that the error-prone mismatch repair machinery preferentially targets top-strand uracils in a way that promotes SHM during the antibody response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Unniraman, Shyam -- Schatz, David G -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1227-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Immunobiology, Yale University School of Medicine, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761884" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/metabolism ; Animals ; B-Lymphocytes ; Base Sequence ; Cytidine Deaminase/*metabolism ; Cytosine/*metabolism ; DNA Mismatch Repair ; Deamination ; *Genes, Immunoglobulin ; Immunoglobulin Variable Region/genetics ; Immunoglobulin kappa-Chains/genetics ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Somatic Hypermutation, Immunoglobulin ; Thymine/metabolism ; Transgenes ; Uracil/metabolism
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  • 25
    Publication Date: 2007-02-10
    Description: Zhang et al. (Research Articles, 11 November 2005, p. 996) reported that obestatin, a peptide derived from the ghrelin precursor, activated the orphan G protein-coupled receptor GPR39. However, we found that I125-obestatin does not bind GPR39 and observed no effects of obestatin on GPR39-transfected cells in various functional assays (cyclic adenosine monophosphate production, calcium mobilization, and GPR39 internalization). Our results indicate that obestatin is not the cognate ligand for GPR39.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chartrel, N -- Alvear-Perez, R -- Leprince, J -- Iturrioz, X -- Reaux-Le Goazigo, A -- Audinot, V -- Chomarat, P -- Coge, F -- Nosjean, O -- Rodriguez, M -- Galizzi, J P -- Boutin, J A -- Vaudry, H -- Llorens-Cortes, C -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):766; author reply 766.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Sante et de la Recherche Medicale (INSERM), U413, Laboratory of Cellular and Molecular Neuroendocrinology, and European Institute for Peptide Research (IFRMP 23), University of Rouen, 76821 Mont-Saint-Aignan, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289961" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CHO Cells ; Calcium/metabolism ; Cell Membrane/metabolism ; Colforsin/pharmacology ; Cricetinae ; Cricetulus ; Cyclic AMP/metabolism ; Ghrelin ; Humans ; Ligands ; Molecular Sequence Data ; Peptide Hormones/genetics/*metabolism/pharmacology ; Pituitary Gland/cytology/metabolism ; Protein Binding ; Receptors, G-Protein-Coupled/genetics/*metabolism ; Transfection
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  • 26
    Publication Date: 2007-01-06
    Description: Dendritic cells (DCs) process and present self and foreign antigens to induce tolerance or immunity. In vitro models suggest that induction of immunity is controlled by regulating the presentation of antigen, but little is known about how DCs control antigen presentation in vivo. To examine antigen processing and presentation in vivo, we specifically targeted antigens to two major subsets of DCs by using chimeric monoclonal antibodies. Unlike CD8+ DCs that express the cell surface protein CD205, CD8- DCs, which are positive for the 33D1 antigen, are specialized for presentation on major histocompatibility complex (MHC) class II. This difference in antigen processing is intrinsic to the DC subsets and is associated with increased expression of proteins involved in MHC processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dudziak, Diana -- Kamphorst, Alice O -- Heidkamp, Gordon F -- Buchholz, Veit R -- Trumpfheller, Christine -- Yamazaki, Sayuri -- Cheong, Cheolho -- Liu, Kang -- Lee, Han-Woong -- Park, Chae Gyu -- Steinman, Ralph M -- Nussenzweig, Michel C -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):107-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, 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/17204652" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; *Antigen Presentation ; Antigens, CD/analysis/immunology ; Antigens, CD8/analysis/immunology ; Base Sequence ; Dendritic Cells/*immunology ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class II/immunology ; Lectins, C-Type/analysis/immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mice, Transgenic ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Receptors, Cell Surface/analysis/immunology ; T-Lymphocytes/immunology
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: A comparison between eukaryotic gene sequences and protein sequences of homologous enzymes from bacterial and mammalian organisms shows that intron-exon junctions frequently coincide with variable surface loops of the protein structures. The altered surface structures can account for functional differences among the members of a family. Sliding of the intron-exon junctions may constitute one mechanism for generating length polymorphisms and divergent sequences found in protein families. Since intron-exon junctions map to protein surfaces, the alterations mediated by sliding of these junctions can be effected without disrupting the stability of the protein core.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Rutter, W J -- Fletterick, R -- AM21344/AM/NIADDK NIH HHS/ -- AM26081/AM/NIADDK NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344214" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological Evolution ; DNA/genetics ; Endopeptidases/genetics ; Eukaryotic Cells/metabolism ; Genes ; Genes, Bacterial ; Protein Conformation ; Proteins/*genetics ; *Serine Endopeptidases ; Tetrahydrofolate Dehydrogenase/genetics
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: An important question concerning the mechanism of somatic mutation of immunoglobulin variable (V) genes is whether it involves all of the numerous V genes in a differentiated B cell, independent of location, or if it is restricted to a particular chromosomal site. Comparison of the sequence of two alleles of a given V gene shows that the mutations are limited to the rearranged V gene, while the same V gene on the other chromosome has not undergone mutation. This indicates that a V gene sequence alone is not sufficient for somatic mutation to take place. The mutation is therefore restricted to the rearranged V gene and consequently does not occur before rearrangement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorski, J -- Rollini, P -- Mach, B -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1179-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites, Antibody/*genetics ; Chromosomes/physiology ; DNA/genetics ; *Genes ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Variable Region/*genetics ; Immunoglobulins/genetics ; Lymphocytes/metabolism ; Mice ; *Mutation
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  • 29
    Publication Date: 1983-06-24
    Description: The size of the Epstein-Barr virus (EBV) nuclear antigen (EBNA) in cells infected with different EBV isolates varies directly with the size of the EBV triplet repeat array, IR3. The isolate with the largest IR3 fragment has approximately 170 more codons than the isolates with the smallest IR3 fragment; it encodes an EBNA which is approximately 17,000 daltons larger than the smallest EBNA. The EBV IR3 encodes part of a 2-kilobase exon of a latently infected cell messenger RNA which must be translated into a repetitive amino acid domain of EBNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hennessy, K -- Heller, M -- van Santen, V -- Kieff, E -- CA 17281/CA/NCI NIH HHS/ -- CA 19264/CA/NCI NIH HHS/ -- GM 07183/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jun 24;220(4604):1396-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304878" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/*genetics ; Base Sequence ; Cell Nucleus/immunology ; DNA, Viral/*genetics ; Epstein-Barr Virus Nuclear Antigens ; Herpesvirus 4, Human/*genetics/immunology ; Humans ; Mice ; RNA, Viral/genetics
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-18
    Description: Polynucleotide templates containing C (cytidine) as the major component facilitate the synthesis of oligonucleotides from mixtures of the activated mononucleotide derivatives (as indicated by structure 1 in the text). A nucleotide is incorporated into oligomeric products if and only if its complement is present in the template. The reaction has a high fidelity and produces products with mean chain lengths of six to ten nucleotides. Bases other than guanosine are incorporated within oligomers or at their 3' termini, but rarely at their 5' termini.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inoue, T -- Orgel, L E -- GM-13435/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Feb 18;219(4586):859-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186026" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Directed RNA Polymerases/*metabolism ; Hydrogen Bonding ; Models, Chemical ; RNA/*chemical synthesis ; Templates, Genetic
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-01
    Description: Oligonucleotide-directed site-specific mutagenesis was applied to alter the cleavage site in the signal peptide of the major outer membrane lipoprotein of Escherichia coli. Replacing the glycine residue at the cleavage site with an alanine residue did not affect the processing of the signal peptide. However, when the same cleavage site was constructed by the deletion of the glycine residue, the signal peptide was no longer cleaved. These results indicate that stringent structural integrity at the cleavage site in the lipoprotein signal sequence is required for correct processing of prolipoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Hsu, C P -- Itakura, K -- Inouye, M -- GM19043/GM/NIGMS NIH HHS/ -- GM30395/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):59-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Outer Membrane Proteins ; Base Sequence ; DNA, Bacterial/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Lipoproteins/*biosynthesis ; Membrane Proteins/biosynthesis ; Mutation ; Protein Precursors/*biosynthesis
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-01-07
    Description: The illustration that accompanied the review by C. C. Albritton, Jr., of W. H. Goetzmann and K. Sloan's Looking Far North (Viking, New York, 1982) in the issue of 10 December, page 1109, should have been credited to the Bancroft Library, University of California, Berkeley, as well as to the book under review.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerman, L S -- New York, N.Y. -- Science. 1983 Jan 7;219(4580):10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6184778" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; RNA/*physiology ; RNA, Small Nuclear
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1983 Mar 4;219(4588):1052-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186029" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/physiology ; DNA/*genetics ; Humans ; Poly A/genetics ; RNA/*genetics ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: The prospects for protein engineering, including the roles of x-ray crystallography, chemical synthesis of DNA, and computer modelling of protein structure and folding, are discussed. It is now possible to attempt to modify many different properties of proteins by combining information on crystal structure and protein chemistry with artificial gene synthesis. Such techniques offer the potential for altering protein structure and function in ways not possible by any other method.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmer, K M -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):666-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6572017" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallography ; Genes ; *Genetic Engineering ; Models, Molecular ; Molecular Biology/trends ; Protein Conformation ; Proteins/*genetics ; X-Ray Diffraction
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: Enhancers, or activators, dramatically increase the transcriptional activity of certain eukaryotic genes. A series of multiple point mutations affecting the simian virus 40 (SV40) enhancer-activator region were generated in order to define the nucleotide sequence required for this function. Three independent assays provided information leading to the identification of nucleotides essential for enhancer function. One class leads to a decrease in gene expression, while the second completely abolishes functional activity. One critical replacement appears to be the first G (guanine) in a sequence TGGAAAG (T, thymine, A, adenine) located in the 5' region of the 72 base-pair repeat of SV40. Comparison of this sequence with nucleotide sequences in other known enhancers leads to the identification of potential related core elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiher, H -- Konig, M -- Gruss, P -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):626-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297005" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Replication ; *Gene Expression Regulation ; Mutation ; *Operon ; Plasmids ; Repetitive Sequences, Nucleic Acid ; Simian virus 40/*genetics ; Virus Replication
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Prokaryotic gene control signals can be isolated, compared, and characterized by precise fusion in vitro to the Escherichia coli galactokinase gene (galK), which provides both a simple assay and genetic selection. This recombinant galK fusion vector system was applied to the study of promoters and terminators recognized by the Escherichia coli RNA polymerase. Three promoters created by mutation from DNA sequences having no promoter function were characterized. Mutations that inactivate promoter function were selected, structurally defined, and functionally analyzed. Similarly, transcription termination was examined, and mutations affecting terminator function were isolated and characterized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, M -- Chepelinsky, A B -- McKenney, K -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):734-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356355" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Bacterial/*genetics ; DNA, Recombinant ; DNA-Directed RNA Polymerases/genetics ; Escherichia coli/genetics ; Galactokinase/genetics ; Gene Expression Regulation ; Mutation ; Nucleic Acid Conformation ; *Operon ; *Transcription, Genetic
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  • 37
    Publication Date: 1983-07-15
    Description: The structure of the messenger RNA (mRNA) encoding the precursor to mouse submaxillary epidermal growth factor (EGF) was determined from the sequence of a set of overlapping complementary DNA's (cDNA). The mRNA is unexpectedly large, about 4750 nucleotide bases, and predicts the sequence of preproEGF, a protein of 1217 amino acids (133,000 molecular weight). The EGF moiety (53 amino acids) is flanked by polypeptide segments of 976 and 188 amino acids at its amino and carboyxl termini, respectively. The amino terminal segment of the precursor contains seven peptides with sequences that are similar but not identical to EGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J -- Urdea, M -- Quiroga, M -- Sanchez-Pescador, R -- Fong, N -- Selby, M -- Rutter, W J -- Bell, G I -- 21344/PHS HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):236-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6602382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Epidermal Growth Factor/biosynthesis/*genetics ; Humans ; Male ; Mice ; RNA, Messenger/*genetics ; Submandibular Gland/metabolism
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-01-14
    Description: Two plasmids containing nonoverlapping deletions of the herpes simplex virus thymidine kinase gene were introduced into thymidine kinase-deficient mouse L cells by DNA-mediated gene transfer. Thymidine kinase-producing transformants were generated by a mixture of the two plasmids at a frequency significantly greater than that generated by either plasmid alone. Southern blot analyses demonstrated that functional thymidine kinase genes were generated by homologous recombination between the two deletion mutants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Small, J -- Scangos, G -- New York, N.Y. -- Science. 1983 Jan 14;219(4581):174-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6294829" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Chromosome Deletion ; *Genetic Engineering ; Mice ; Mutation ; *Plasmids ; *Recombination, Genetic ; Simplexvirus ; Thymidine Kinase/*genetics
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Comparison of two closely related primate papovaviruses, simian virus 40 (SV40) and human BK virus (BKV), reveals that the only region of extensive divergence, the tandem sequences adjacent to the origins of DNA replication, is responsible in SV40 for enhancing early gene expression. This study demonstrates a similar enhancer function for the analogous repeated region in BKV. The dissimilarity in sequence of the BKV and SV40 enhancer elements suggests that they may have been acquired since SV40 and BKV diverged. A locus cloned from the human genome homologous to the BKV tandem repeats has been shown to function as low level enhancer element in mammalian cells. These data support the hypothesis that viral enhancer sequences may be evolutionarily related to host cell sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenthal, N -- Kress, M -- Gruss, P -- Khoury, G -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):749-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BK Virus/*genetics ; Base Sequence ; Biological Evolution ; DNA, Viral/*genetics ; Gene Expression Regulation ; *Genes, Regulator ; Humans ; Plasmids ; Polyomavirus/*genetics ; Repetitive Sequences, Nucleic Acid ; Species Specificity
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  • 40
    Publication Date: 1983-06-03
    Description: In order to investigate the functions of stimulus recognition, signal transduction, and adaptation, the aspartate receptor gene for bacterial chemotaxis in Salmonella typhimurium has been sequenced and modified. A carboxyl-terminal truncated receptor was shown to bind aspartate and to transmit a signal to change motility behavior. However, the truncated receptor showed greatly reduced methyl-accepting capacity, and did not allow adaptation to the sensory stimulation. The separation of receptor functions by alteration of primary structure emphasizes that the receptor is directly involved in adaptation and is not solely a device for transmitting a signal across a membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russo, A F -- Koshland, D E Jr -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1016-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302843" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Aspartic Acid ; *Bacterial Physiological Phenomena ; Base Sequence ; *Chemotaxis ; Escherichia coli/physiology ; Methylation ; *Receptors, Amino Acid ; Receptors, Cell Surface/genetics/*physiology ; Salmonella typhimurium/physiology ; Serine
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Insertion sequences (IS) are discrete segments of DNA that can transpose from one genomic site to another and promote genetic rearrangements. A question that is central to understanding the mechanism of transpositional recombination is whether genetic rearrangements are accompanied by duplication of the IS that promotes them. Analysis of adjacent deletions mediated by IS903 provides the strongest evidence to date than any IS-mediated transpositional recombination can occur by an efficient replicative mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinert, T A -- Schaus, N A -- Grindley, N D -- GM28470/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):755-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314502" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; *DNA Transposable Elements ; DNA, Bacterial/*genetics ; Plasmids ; *Recombination, Genetic ; Repetitive Sequences, Nucleic Acid
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-08-26
    Description: One variant of a complex satellite DNA of the Bermuda land crab is significantly longer than the average repeat unit of the satellite. The extra DNA in the variant is accounted for by a fivefold tandem amplification of a 0.142-kilobase sequence. The amplified sequence is bounded by a tetranucleotide inverted repeat; the upstream arm of the inverted repeat is missing from two other variants of the satellite. The latter variants contain only one copy of a sequence that is closely related to the amplified sequence. By contrast, in several satellite DNA's of other organisms, extra DNA is inserted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonnewell, V -- Fowler, R F -- Skinner, D M -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):862-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6879182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Brachyura/genetics ; Chromosome Inversion ; DNA, Satellite/*genetics ; *Gene Amplification ; Nucleic Acid Conformation
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  • 43
    Publication Date: 1983-07-15
    Description: The polymorphism of immune response genes plays a critical role in determining the immune capabilities of a particular individual. The molecular nature of this polymorphism was studied by examining the structure of the coding portions of three alleles of the I-A beta chain gene, an immune response gene whose protein product constitutes a subunit of the I-A molecule. Comparison of the I-A beta chains encoded by these alleles revealed an amino acid sequence divergence of 5 to 8 percent. The differences were found to be a series of short alterations clustered in the amino terminal half of the polypeptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, E -- McIntyre, K -- Germain, R N -- Seidman, J G -- AI18436/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):283-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6407114" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; *Genes, MHC Class II ; Histocompatibility Antigens Class II/immunology ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; *Polymorphism, Genetic
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-27
    Description: The utility of somatic cell genetic analysis for the chromosomal localization of genes in mammals is well established. With the development of recombinant DNA probes and efficient blotting techniques that allow visualization of single-copy cellular genes, somatic cell genetics has been extended from the level of phenotypes expressed by whole cells to the level of the cellular genome itself. This extension has proved invaluable for the analysis of genes not readily expressed in somatic cell hybrids and for the study of multigene families, especially pseudogenes dispersed in different chromosomes throughout the genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Eustachio, P -- Ruddle, F H -- GM-09966/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 May 27;220(4600):919-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6573776" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Human ; Cricetinae ; Cricetulus ; DNA, Recombinant/metabolism ; Genes ; Genetic Markers ; Genetics ; Humans ; Hybrid Cells/metabolism ; Mice ; Polymorphism, Genetic ; RNA, Messenger/metabolism
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Class III genes require multiple cellular factors for transcription by RNA polymerase III; these genes form stable transcription complexes, which in the case of Xenopus 5S genes are correlated with differential expression in vivo. The minimal number and identity of the factors required to form both stable and metastable complexes on three class III genes (encoding, respectively, 5S RNA, transfer RNA, and adenovirus VA RNA species) were determined. Stable complex formation requires one common factor, whose recognition site was analyzed, and either no additional factors (the VA gene), a second common factor (the transfer RNA gene), or a third gene-specific factor (the 5S gene). The mechanism of stable complex formation and its relevance to transcriptional regulation were examined in light of the various factors and the promoter sequences recognized by these factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lassar, A B -- Martin, P L -- Roeder, R G -- CA 24223/CA/NCI NIH HHS/ -- CA 24891/CA/NCI NIH HHS/ -- GM07200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):740-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356356" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA-Directed RNA Polymerases/*genetics ; Eukaryotic Cells/physiology ; Gene Expression Regulation ; Genes ; Humans ; Operon ; RNA Polymerase III/*genetics ; RNA, Ribosomal/genetics ; RNA, Transfer/genetics ; RNA, Viral/genetics ; Transcription Factors/genetics ; *Transcription, Genetic
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-08-19
    Description: Ia (I region-associated) antigens are cell-surface glycoproteins involved in the regulation of immune responsiveness. They are composed of one heavy (alpha) and one light (beta) polypeptide chain. We have sequenced the gene encoding the A beta d chain of the BALB/c mouse. The presence of six exons is predicted by comparison with the complementary DNA sequences of human beta chains and with partial protein sequence data for the A beta d polypeptide. Sequence comparisons have been made to other proteins involved in immune responses and the consequent implications for the evolutionary relationships of these genes are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malissen, M -- Hunkapiller, T -- Hood, L -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):750-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6410508" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Codon ; Genes ; *Genes, MHC Class II ; Macromolecular Substances ; Major Histocompatibility Complex ; Mice ; beta 2-Microglobulin/genetics
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  • 47
    Publication Date: 1983-11-04
    Description: The gene for glycoprotein D of herpes simplex virus type 1 (HSV-1) was expressed in stable mammalian cell lines. Glycoprotein D produced in these cells has a number of antigenic determinants in common with the native glycoprotein. Cell lines expressing glycoprotein D were used in an enzyme-linked immunosorbent assay to detect human antibodies to glycoprotein D. This strategy should prove useful in determining the extent to which the immune response to HSV-1 is directed toward glycoprotein D.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berman, P W -- Dowbenko, D -- Lasky, L A -- Simonsen, C C -- New York, N.Y. -- Science. 1983 Nov 4;222(4623):524-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6312563" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Viral/*analysis ; Base Sequence ; Cell Line ; Clone Cells ; DNA Restriction Enzymes ; DNA, Viral/genetics ; Enzyme-Linked Immunosorbent Assay ; *Genes ; *Genes, Viral ; Humans ; Plasmids ; Simplexvirus/genetics/*immunology ; Tetrahydrofolate Dehydrogenase/genetics ; *Viral Envelope Proteins ; Viral Proteins/*genetics/immunology
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1983 Nov 25;222(4626):915.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314505" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA Transposable Elements ; Viroids/*genetics
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  • 49
    Publication Date: 1983-08-26
    Description: The complete nucleotide sequence of the diphtheria tox228 gene encoding the nontoxic serologically related protein CRM228 has been determined. A comparison of the predicted amino acid sequence with the available amino acid sequences from the wild-type toxin made it possible to deduce essentially the entire nucleotide sequence of the wild-type tox gene. The signal peptide of pro-diphtheria toxin and the putative tox promoter have been identified, a highly symmetrical nucleotide sequence downstream of the toxin gene has been detected; this region may be the corynebacteriophage beta attachment site (attP). The cloned toxin gene was expressed at a low level in Escherichia coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaczorek, M -- Delpeyroux, F -- Chenciner, N -- Streeck, R E -- Murphy, J R -- Boquet, P -- Tiollais, P -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):855-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6348945" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; Diphtheria Toxin/*genetics ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; Nucleic Acid Conformation ; Operon
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-24
    Description: Human G gamma-globin genes containing tandem duplications of the donor (5') or acceptor (3') RNA splice sites of the second intervening sequence were constructed in order to ascertain the directionality of RNA splice site selection. These genes were introduced into cultured monkey cells, and their transcripts were analyzed. Transcripts of these duplication variants were spliced only at the proximal copy of the duplicated splice sites. These data are consistent with a 5' leads to 3' model of splice site selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lang, K M -- Spritz, R A -- AM28598/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 24;220(4604):1351-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304877" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Globins/genetics ; Haplorhini ; Humans ; Plasmids ; *RNA Splicing ; RNA, Messenger/genetics/physiology ; Simian virus 40/genetics ; Transcription, Genetic
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-08
    Description: The nucleotide sequence of the oncogene of the Rasheed strain of rat sarcoma virus was determined. The oncogene (Ra-v-ras) encodes a 29,000-dalton (p29) transforming protein. This protein is distinct from the immunologically related 21,000-dalton protein (p21) of the Harvey murine sarcoma virus in its amino terminus and in having additional mutations in its carboxyl terminus. Although the functional significance of these changes is unknown, they appear to occur only in rat sarcoma virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasheed, S -- Norman, G L -- Heidecker, G -- CA 27246/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 8;221(4606):155-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344220" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Proto-Oncogene Proteins p21(ras) ; Rats ; Retroviridae/*genetics
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-03
    Description: The nucleotide sequence of the T24 human bladder carcinoma oncogene was determined, and the coding and noncoding sequences of the genome were identified. The amino acid sequence of p21, the translational product of the T24 oncogene, was predicted from the nucleotide sequence of the oncogene. Comparison of this sequence with that of the normal cellular homolog showed that a single point mutation in the coding sequences of the T24 oncogene resulted in the acquisition of transforming properties. Other differences between the T24 oncogene and its normal cellular homolog were found in the 5' noncoding and 3' noncoding sequences, but these differences appear to be due to polymorphism and do not play a significant role in the transformation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1061-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6844927" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinoma/*genetics ; Cell Transformation, Neoplastic/metabolism ; Humans ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Oncogenic Viruses/genetics ; Rats ; Urinary Bladder Neoplasms/*genetics
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  • 53
    Publication Date: 1983-05-13
    Description: A recombinant bacterial plasmid, pMS1, was constructed that contains 318 nucleotides complementary to a portion of pro-opiolipomelanocortin (proOLMC) messenger RNA from an ectopic adrenocorticotropin-producing tumor. The cloned complementary DNA insert, which contains the sequence that codes for all of the beta-melanocyte-stimulating hormone and beta-endorphin portions of proOLMC, as well as the 3' nontranslated section, is identical to the genomic sequence. Hybridization of tumor proOLMC complementary DNA to RNA subjected to electrophoresis and transferred to a nitrocellulose filter revealed two proOLMC messenger RNA species in the tumor polyadenylated RNA, but only one in pituitary polyadenylated RNA. At least one of the tumor proOLMC messenger RNA's is similar, if not identical, to human pituitary proOLMC messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeBold, C R -- Schworer, M E -- Connor, T B -- Bird, R E -- Orth, D N -- 2-R01-GM25526/GM/NIGMS NIH HHS/ -- 5-R01-CA11685/CA/NCI NIH HHS/ -- 5-R25-CA19429/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 May 13;220(4598):721-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6301015" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carcinoid Tumor/physiopathology ; Cloning, Molecular ; DNA, Neoplasm/genetics ; DNA, Recombinant/*metabolism ; Endorphins/*genetics ; Hormones, Ectopic/*genetics ; Humans ; Male ; Melanocyte-Stimulating Hormones/*genetics ; Middle Aged ; Pancreatic Neoplasms/physiopathology ; Pituitary Hormones, Anterior/*genetics ; Pro-Opiomelanocortin ; Protein Precursors/*genetics ; RNA, Messenger/genetics ; beta-Endorphin
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  • 54
    Publication Date: 1983-11-18
    Description: The characteristic chromosomal translocations that occur in certain human malignancies offer opportunities to understand how two gene systems can affect one another when they are accidentally juxtaposed. In the case of Burkitt lymphoma, such a translocation joins the cellular oncogene, c-myc, to a region encoding one of the immunoglobulin genes. In at least one example, the coding sequence of the rearranged c-myc gene is identical to that of the normal gene, implying that the gene must be quantitatively, rather than qualitatively, altered in its expression if it is to play a role in transformation. One might expect to find the rearranged c-myc gene in a configuration that would allow it to take advantage of one of the known immunoglobulin promoters or enhancer elements. However, the rearranged c-myc gene is often placed so that it can utilize neither of these structures. Since the level of c-myc messenger RNA is often elevated in Burkitt cells, the translocation may lead to a deregulation of the c-myc gene. Further, since the normal allele in a Burkitt cell is often transcriptionally silent in the presence of a rearranged allele, a model for c-myc regulation is suggested that involves a trans-acting negative control element that might use as its target a highly conserved portion of the c-myc gene encoding two discrete transcriptional promoters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leder, P -- Battey, J -- Lenoir, G -- Moulding, C -- Murphy, W -- Potter, H -- Stewart, T -- Taub, R -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):765-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356357" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Burkitt Lymphoma/*genetics ; Cell Transformation, Neoplastic/etiology ; Chromosome Aberrations/*genetics ; Chromosome Disorders ; Chromosome Mapping ; Gene Expression Regulation ; Genes ; Humans ; Immunoglobulins/genetics ; Models, Biological ; Neoplasms/*genetics ; *Oncogenes ; *Translocation, Genetic
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  • 55
    Publication Date: 1983-02-04
    Description: The 5' nucleotide sequences of the transforming gene of simian sarcoma virus (v-sis) and its human cellular homolog (c-sis) were compared. A short homology was found between helper virus and cellular DNA sequences at the junction of v-sis and c-sis, which may have had a role in the original recombination event leading to the generation of simian sarcoma virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Josephs, S F -- Dalla-Favera, R -- Gelmann, E P -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1983 Feb 4;219(4584):503-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297002" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Genes, Viral ; Helper Viruses/genetics ; Humans ; *Oncogenes ; Recombination, Genetic ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics
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  • 56
    Publication Date: 1983-02-18
    Description: The c-ras1H oncogene can be distinguished from its normal cellular counterpart by the loss of a restriction endonuclease site. This sequence alteration is the basis of a rapid screening method for the presence of this oncogene. DNA's from 34 individuals were screened by this method, and all were homozygous for the normal allele. In contrast, DNA from a patient's bladder tumor, as well as DNA from his normal bladder and leukocytes, were heterozygous at that restriction endonuclease site. Further restriction enzyme mapping pinpointed the change in the mutant allele as being one of two nucleotides, either of which would change the 12th amino acid (glycine) in the normal c-ras1H gene product. Point mutations in the codon for this amino acid have previously been described in a bladder tumor cell line and in the viral oncogene v-rasH. These results indicate that the patient carried a c-ras1H oncogene in his germ line, raising the possibility that the c-ras1H oncogene confers a predisposition to neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muschel, R J -- Khoury, G -- Lebowitz, P -- Koller, R -- Dhar, R -- New York, N.Y. -- Science. 1983 Feb 18;219(4586):853-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6337398" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Transformation, Neoplastic/pathology ; Humans ; Mutation ; *Oncogenes ; Urinary Bladder Neoplasms/*genetics
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-22
    Description: Nucleotide sequences of translated regions of the trp operon in 12 wild strains of Escherichia coli reveal striking uniformity among eight strains (suggesting recent common ancestry and supporting the importance of periodic selection in natural populations) and clustered substitutions in four strains (implicating events affecting runs of nucleotides).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milkman, R -- Crawford, I P -- New York, N.Y. -- Science. 1983 Jul 22;221(4608):378-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6346486" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Bacterial/genetics ; Escherichia coli/*genetics ; Genes, Bacterial
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  • 58
    Publication Date: 1983-07-01
    Description: With a synthetic oligonucleotide mixture as probe, complementary DNA clones of C-reactive protein were isolated from an adult human liver complementary DNA library. The clones ranged in size from 700 to 1100 base pairs and were identified by partial DNA sequence analysis. One complementary DNA clone was used as a probe for hybridization with human-rodent DNA's isolated from somatic cell hybrids and bound to nitrocellulose filters (Southern blot analysis) to assign the human C-reactive protein gene to chromosome 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitehead, A S -- Bruns, G A -- Markham, A F -- Colten, H R -- Woods, D E -- AI15033/AI/NIAID NIH HHS/ -- HD4807/HD/NICHD NIH HHS/ -- HL22487/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):69-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; C-Reactive Protein/*genetics ; *Chromosome Mapping ; *Chromosomes, Human, 1-3 ; Cloning, Molecular ; Cricetinae ; DNA/*genetics/isolation & purification ; Genes ; Humans ; Hybrid Cells/metabolism ; Mice
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  • 59
    Publication Date: 1983-11-18
    Description: Three mutations of the enzyme dihydrofolate reductase were constructed by oligonucleotide-directed mutagenesis of the cloned Escherichia coli gene. The mutations--at residue 27, aspartic acid replaced with asparagine; at residue 39, proline replaced with cysteine; and at residue 95, glycine replaced with alanine--were designed to answer questions about the relations between molecular structure and function that were raised by the x-ray crystal structures. Properties of the mutant proteins show that Asp-27 is important for catalysis and that perturbation of the local structure at a conserved cis peptide bond following Gly-95 abolishes activity. Substitution of cysteine for proline at residue 39 results in the appearance of new forms of the enzyme that correspond to various oxidation states of the cysteine. One of these forms probably represents a species cross-linked by an intrachain disulfide bridge between the cysteine at position 85 and the new cysteine at position 39.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Villafranca, J E -- Howell, E E -- Voet, D H -- Strobel, M S -- Ogden, R C -- Abelson, J N -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- F32 GM09375/GM/NIGMS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):782-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Disulfides ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/*genetics
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