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  • Calcium
  • Immunocytochemistry
  • Saccharomyces cerevisiae
  • Springer  (1,133)
  • American Association for the Advancement of Science (AAAS)  (16)
  • American Chemical Society (ACS)
  • American Meteorological Society
  • Blackwell Publishing Ltd
  • International Union of Crystallography
  • Public Library of Science
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  • 1
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    Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-31
    Description: Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves specific uptake into coat protein complex II (COPII)-coated vesicles of secretory and of vesicle targeting (v-SNARE) proteins. Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specifically with Sar1p, Sec23p, and Sec24p, components of the COPII coat, in a guanine nucleotide-dependent fashion. Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p. The data suggest that transmembrane proteins can be taken up into COPII vesicles by direct interactions with the coat proteins and may play a structural role in the assembly of the COPII coat complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Springer, S -- Schekman, R -- New York, N.Y. -- Science. 1998 Jul 31;281(5377):698-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720-3202, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9685263" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; COP-Coated Vesicles ; Carrier Proteins/*metabolism ; Endoplasmic Reticulum/*metabolism ; Fungal Proteins/*metabolism ; GTP Phosphohydrolases/metabolism ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; Golgi Apparatus/*metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Guanylyl Imidodiphosphate/metabolism/pharmacology ; Membrane Proteins/*metabolism ; *Membrane Transport Proteins ; *Monomeric GTP-Binding Proteins ; Qb-SNARE Proteins ; Qc-SNARE Proteins ; R-SNARE Proteins ; Receptors, Cell Surface/metabolism ; Recombinant Fusion Proteins/metabolism ; SNARE Proteins ; Saccharomyces cerevisiae ; *Saccharomyces cerevisiae Proteins ; *Vesicular Transport Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Complex grabbing (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-10-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikorski, R -- Peters, R -- New York, N.Y. -- Science. 1999 Sep 17;285(5435):1868.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10515792" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Genetic Techniques ; Protein Binding ; Proteins/*isolation & purification/metabolism ; Recombinant Fusion Proteins/metabolism ; Ribonucleoproteins, Small Nuclear/metabolism ; Saccharomyces cerevisiae ; Sequence Analysis/*methods
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    A copper cofactor for the ethylene receptor ETR1 from Arabidopsis (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-02-12
    Description: The ETR1 receptor from Arabidopsis binds the gaseous hormone ethylene. A copper ion associated with the ethylene-binding domain is required for high-affinity ethylene-binding activity. A missense mutation in the domain that renders the plant insensitive to ethylene eliminates both ethylene binding and the interaction of copper with the receptor. A sequence from the genome of the cyanobacterium Synechocystis sp. strain 6803 that shows homology to the ethylene-binding domain of ETR1 encodes a functional ethylene-binding protein. On the basis of sequence conservation between the Arabidopsis and the cyanobacterial ethylene-binding domains and on in vitro mutagenesis of ETR1, a structural model for this copper-based ethylene sensor domain is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodriguez, F I -- Esch, J J -- Hall, A E -- Binder, B M -- Schaller, G E -- Bleecker, A B -- New York, N.Y. -- Science. 1999 Feb 12;283(5404):996-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, 430 Lincoln Drive, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9974395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Arabidopsis/genetics/*metabolism ; Bacterial Proteins/chemistry/genetics ; Binding Sites ; Conserved Sequence ; Copper/analysis/*metabolism ; Copper Sulfate/pharmacology ; Cyanobacteria/genetics/metabolism ; Dimerization ; Ethylenes/*metabolism ; Models, Molecular ; Mutagenesis ; Open Reading Frames ; Plant Proteins/chemistry/genetics/isolation & purification/*metabolism ; Receptors, Cell Surface/chemistry/genetics/isolation & purification/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae ; Silver/metabolism/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-26
    Description: The SWI/SNF complex participates in the restructuring of chromatin for transcription. The function of the yeast SWI/SNF complex in the remodeling of a nucleosome array has now been analyzed in vitro. Binding of the purified SWI/SNF complex to a nucleosome array disrupted multiple nucleosomes in an adenosine triphosphate-dependent reaction. However, removal of SWI/SNF left a deoxyribonuclease I-hypersensitive site specifically at a nucleosome that was bound by derivatives of the transcription factor Gal4p. Analysis of individual nucleosomes revealed that the SWI/SNF complex catalyzed eviction of histones from the Gal4-bound nucleosomes. Thus, the transient action of the SWI/SNF complex facilitated irreversible disruption of transcription factor-bound nucleosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owen-Hughes, T -- Utley, R T -- Cote, J -- Peterson, C L -- Workman, J L -- GM47867/GM/NIGMS NIH HHS/ -- R01 GM049650/GM/NIGMS NIH HHS/ -- R37 GM049650/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):513-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology and Center for Gene Regulation, Pennsylvania State University, University Park, PA 16802-4500, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662543" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases ; Adenosine Triphosphate/metabolism ; Base Sequence ; Binding Sites ; DNA, Fungal/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Fungal Proteins/*metabolism ; Histones/metabolism ; Molecular Sequence Data ; *Nuclear Proteins ; Nucleosomes/*metabolism/ultrastructure ; Saccharomyces cerevisiae ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Zinc-dependent structure of a single-finger domain of yeast ADR1 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-16
    Description: In the proposed "zinc finger" DNA-binding motif, each repeat unit binds a zinc metal ion through invariant Cys and His residues and this drives the folding of each 30-residue unit into an independent nucleic acid-binding domain. To obtain structural information, we synthesized single and double zinc finger peptides from the yeast transcription activator ADR1, and assessed the metal-binding and DNA-binding properties of these peptides, as well as the solution structure of the metal-stabilized domains, with the use of a variety of spectroscopic techniques. A single zinc finger can exist as an independent structure sufficient for zinc-dependent DNA binding. An experimentally determined model of the single finger is proposed that is consistent with circular dichroism, one- and two-dimensional nuclear magnetic resonance, and visual spectroscopy of the single-finger peptide reconstituted in the presence of zinc.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parraga, G -- Horvath, S J -- Eisen, A -- Taylor, W E -- Hood, L -- Young, E T -- Klevit, R E -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1489-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3047872" target="_blank"〉PubMed〈/a〉
    Keywords: Circular Dichroism ; DNA Mutational Analysis ; *DNA-Binding Proteins ; Magnetic Resonance Spectroscopy ; Metalloproteins ; Protein Conformation ; Saccharomyces cerevisiae ; Structure-Activity Relationship ; *Transcription Factors ; Zinc/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Clathrin: a role in the intracellular retention of a Golgi membrane protein (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-09-22
    Description: Yeast mutants deficient in the clathrin heavy chain secrete a precursor form of the alpha-factor, a peptide-mating pheromone. Analysis of this defect indicates that the endoprotease Kex2p, which is responsible for initiating proteolytic maturation of the alpha-factor precursor in the Golgi apparatus, is unexpectedly present at the plasma membrane in mutant cells. This result suggest that clathrin is required for the retention of Kex2p in the Golgi apparatus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Payne, G S -- Schekman, R -- GM 36881/GM/NIGMS NIH HHS/ -- GM 39040/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Sep 22;245(4924):1358-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, UCLA School of Medicine 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2675311" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Compartmentation ; Clathrin/*physiology ; Golgi Apparatus/*physiology ; Intracellular Membranes/*physiology ; Membrane Proteins/*physiology ; Peptide Hydrolases/metabolism ; Peptides/metabolism ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae
    Print ISSN: 0036-8075
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  • 7
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    An early hierarchic role of U1 small nuclear ribonucleoprotein in spliceosome assembly (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: Splicing of nuclear precursor messenger RNA (pre-mRNA) occurs on a large ribonucleoprotein complex, the spliceosome. Several small nuclear ribonucleoproteins (snRNP's) are subunits of this complex that assembles on the pre-mRNA. Although the U1 snRNP is known to recognize the 5' splice site, its roles in spliceosome formation and splice site alignment have been unclear. A new affinity purification method for the spliceosome is described which has provided insight into the very early stages of spliceosome formation in a yeast in vitro splicing system. Surprisingly, the U1 snRNP initially recognizes sequences at or near both splice junctions in the intron. This interaction must occur before the other snRNP's (U2, U4, U5, and U6) can join the complex. The results suggest that interaction of the two splice site regions occurs at an early stage of spliceosome formation and is probably mediated by U1 snRNP and perhaps other factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruby, S W -- Abelson, J -- GM32637/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1028-35.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2973660" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Adenosine Triphosphate/metabolism ; Cell-Free System ; DNA Mutational Analysis ; Macromolecular Substances ; Protein Binding ; *RNA Splicing ; RNA, Messenger/*physiology ; Ribonucleoproteins/*physiology ; Ribonucleoproteins, Small Nuclear ; Saccharomyces cerevisiae
    Print ISSN: 0036-8075
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  • 8
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    PIN: an associated protein inhibitor of neuronal nitric oxide synthase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-01
    Description: The neurotransmitter functions of nitric oxide are dependent on dynamic regulation of its biosynthetic enzyme, neuronal nitric oxide synthase (nNOS). By means of a yeast two-hybrid screen, a 10-kilodalton protein was identified that physically interacts with and inhibits the activity of nNOS. This inhibitor, designated PIN, appears to be one of the most conserved proteins in nature, showing 92 percent amino acid identity with the nematode and rat homologs. Binding of PIN destabilizes the nNOS dimer, a conformation necessary for activity. These results suggest that PIN may regulate numerous biological processes through its effects on nitric oxide synthase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaffrey, S R -- Snyder, S H -- DA00074/DA/NIDA NIH HHS/ -- GM-07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):774-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864115" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism/pharmacology ; Cell Line ; Cyclic GMP/metabolism ; Dimerization ; *Drosophila Proteins ; Dyneins ; Enzyme Inhibitors/chemistry/*metabolism/pharmacology ; Humans ; Molecular Sequence Data ; Molecular Weight ; Neurons/enzymology ; Nitric Oxide Synthase/*antagonists & inhibitors/metabolism ; Rats ; Recombinant Fusion Proteins/metabolism/pharmacology ; Saccharomyces cerevisiae ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 9
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    Ethylene-binding sites generated in yeast expressing the Arabidopsis ETR1 gene (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: Mutations in the ETR1 gene of Arabidopsis thaliana confer insensitivity to ethylene, which indicates a role for the gene product in ethylene signal transduction. Saturable binding sites for [14C]ethylene were detected in transgenic yeast expressing the ETR1 protein, whereas control yeast lacking ETR1 showed no detectable ethylene binding. Yeast expressing a mutant form of ETR1 (etr1-1) also showed no detectable ethylene binding, which provides an explanation for the ethylene-insensitive phenotype observed in plants carrying this mutation. Expression of truncated forms of ETR1 in yeast provided evidence that the amino-terminal hydrophobic domain of the protein is the site of ethylene binding. It was concluded from these results that ETR1 acts as an ethylene receptor in Arabidopsis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaller, G E -- Bleecker, A B -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1809-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, University of Wisconsin, Madison 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525372" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism ; Binding Sites ; Cloning, Molecular ; Ethylenes/*metabolism ; Genes, Plant ; Mutagenesis, Site-Directed ; Peptide Fragments/genetics/metabolism ; Plant Proteins/genetics/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Recombinant Proteins/genetics/metabolism ; Saccharomyces cerevisiae
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: Trapoxin is a microbially derived cyclotetrapeptide that inhibits histone deacetylation in vivo and causes mammalian cells to arrest in the cell cycle. A trapoxin affinity matrix was used to isolate two nuclear proteins that copurified with histone deacetylase activity. Both proteins were identified by peptide microsequencing, and a complementary DNA encoding the histone deacetylase catalytic subunit (HD1) was cloned from a human Jurkat T cell library. As the predicted protein is very similar to the yeast transcriptional regulator Rpd3p, these results support a role for histone deacetylase as a key regulator of eukaryotic transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taunton, J -- Hassig, C A -- Schreiber, S L -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):408-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Bacterial Agents/metabolism/pharmacology ; Cattle ; Cell Cycle/drug effects ; Cloning, Molecular ; Enzyme Inhibitors/metabolism/pharmacology ; Fungal Proteins/chemistry/genetics/*metabolism ; *Gene Expression Regulation ; Histone Deacetylase Inhibitors ; Histone Deacetylases/chemistry/genetics/isolation & purification/*metabolism ; Humans ; Hydroxamic Acids/metabolism/pharmacology ; Molecular Sequence Data ; Molecular Weight ; *Peptides ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins ; T-Lymphocytes/enzymology ; Transcription Factors/chemistry/genetics/isolation & purification/*metabolism ; *Transcription, Genetic ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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