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  • *Saccharomyces cerevisiae Proteins  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
  • Oxford University Press
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  • American Association for the Advancement of Science (AAAS)  (4)
  • Oxford University Press
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  • 1
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    Genetic selection of peptide inhibitors of biological pathways (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1999-07-27
    Beschreibung: Genetic selections were used to find peptides that inhibit biological pathways in budding yeast. The peptides were presented inside cells as peptamers, surface loops on a highly expressed and biologically inert carrier protein, a catalytically inactive derivative of staphylococcal nuclease. Peptamers that inhibited the pheromone signaling pathway, transcriptional silencing, and the spindle checkpoint were isolated. Putative targets for the inhibitors were identified by a combination of two-hybrid analysis and genetic dissection of the target pathways. This analysis identified Ydr517w as a component of the spindle checkpoint and reinforced earlier indications that Ste50 has both positive and negative roles in pheromone signaling. Analysis of transcript arrays showed that the peptamers were highly specific in their effects, which suggests that they may be useful reagents in organisms that lack sophisticated genetics as well as for identifying components of existing biological pathways that are potential targets for drug discovery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norman, T C -- Smith, D L -- Sorger, P K -- Drees, B L -- O'Rourke, S M -- Hughes, T R -- Roberts, C J -- Friend, S H -- Fields, S -- Murray, A W -- P41-RR11823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 23;285(5427):591-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, CA 94143-0444, USA. tnorman@microbia.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10417390" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Fungal Proteins/metabolism ; G1 Phase ; Galactose/metabolism ; Lipoproteins/metabolism ; Micrococcal Nuclease ; Mitosis ; Molecular Sequence Data ; Peptide Library ; Peptides/genetics/metabolism/*pharmacology ; Pheromones/*metabolism ; Protein Binding ; Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; *Selection, Genetic ; *Signal Transduction ; Spindle Apparatus/drug effects/*metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    Signaling and circuitry of multiple MAPK pathways revealed by a matrix of global gene expression profiles (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2000-02-05
    Beschreibung: Genome-wide transcript profiling was used to monitor signal transduction during yeast pheromone response. Genetic manipulations allowed analysis of changes in gene expression underlying pheromone signaling, cell cycle control, and polarized morphogenesis. A two-dimensional hierarchical clustered matrix, covering 383 of the most highly regulated genes, was constructed from 46 diverse experimental conditions. Diagnostic subsets of coexpressed genes reflected signaling activity, cross talk, and overlap of multiple mitogen-activated protein kinase (MAPK) pathways. Analysis of the profiles specified by two different MAPKs-Fus3p and Kss1p-revealed functional overlap of the filamentous growth and mating responses. Global transcript analysis reflects biological responses associated with the activation and perturbation of signal transduction pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, C J -- Nelson, B -- Marton, M J -- Stoughton, R -- Meyer, M R -- Bennett, H A -- He, Y D -- Dai, H -- Walker, W L -- Hughes, T R -- Tyers, M -- Boone, C -- Friend, S H -- New York, N.Y. -- Science. 2000 Feb 4;287(5454):873-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosetta Inpharmatics, 12040 115th Avenue Northeast, Kirkland, WA 98034, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10657304" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Cell Cycle Proteins ; Cyclin-Dependent Kinase Inhibitor Proteins ; Fungal Proteins/genetics/metabolism/physiology ; G1 Phase ; *Gene Expression Profiling ; *Gene Expression Regulation, Fungal ; Genome, Fungal ; Lipoproteins/pharmacology/physiology ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/metabolism ; Multigene Family ; Oligonucleotide Array Sequence Analysis ; Peptides/pharmacology/physiology ; Pheromones ; Protein Kinase C/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/cytology/*genetics/growth & development/physiology ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/metabolism ; Transcriptional Activation
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
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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
    Publikationsdatum: 1996-07-26
    Beschreibung: 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〉
    Schlagwort(e): 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
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
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    Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1996-10-11
    Beschreibung: The CDC13 gene has previously been implicated in the maintenance of telomere integrity in Saccharomyces cerevisiae. With the use of two classes of mutations, here it is shown that CDC13 has two discrete roles at the telomere. The cdc13-2est mutation perturbs a function required in vivo for telomerase regulation but not in vitro for enzyme activity, whereas cdc13-1ts defines a separate essential role at the telomere. In vitro, purified Cdc13p binds to single-strand yeast telomeric DNA. Therefore, Cdc13p is a telomere-binding protein required to protect the telomere and mediate access of telomerase to the chromosomal terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nugent, C I -- Hughes, T R -- Lue, N F -- Lundblad, V -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):249-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Human Genetics and Cell and Molecular Biology Program, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824190" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alleles ; Base Sequence ; Cloning, Molecular ; Cyclin B ; Cyclins/genetics/*metabolism ; DNA, Fungal/metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/genetics ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Phenotype ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/*metabolism ; Telomere/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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