A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators
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Published in | Molecular and Cellular Biology Vol. 17; no. 8; pp. 4852 - 4858 |
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Format | Journal Article |
Language | English |
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American Society for Microbiology
01.08.1997
Taylor & Francis |
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AbstractList | The SIN3 gene is required for the transcriptional repression of diverse genes in Saccharomyces cerevisiae. Sin3p does not bind directly to DNA but is thought to be targeted to promoters by interacting with sequence-specific DNA-binding proteins. We show here that Sin3p is present in a large multiprotein complex with an apparent molecular mass, estimated by gel filtration chromatography, of greater than 2 million Da. Genetic studies have shown that the yeast RPD3 gene has a function similar to that of SIN3 in transcriptional regulation, as SIN3 and RPD3 negatively regulate the same set of genes. The SIN3 and RPD3 genes are conserved from yeasts to mammals, and recent work suggests that RPD3 may encode a histone deacetylase. We show that Rpd3p is present in the Sin3p complex and that an rpd3 mutation eliminates SIN3-dependent repression. Thus, Sin3p may function as a bridge to recruit the Rpd3p histone deacetylase to specific promoters. Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB |
Author | D J Stillman M M Kasten S Dorland |
AuthorAffiliation | Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah Health Sciences Center, Salt Lake City 84132, USA |
AuthorAffiliation_xml | – name: Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah Health Sciences Center, Salt Lake City 84132, USA |
Author_xml | – sequence: 1 givenname: Margaret M. surname: Kasten fullname: Kasten, Margaret M. organization: Division of Molecular Biology and Genetics, Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah Health Sciences Center – sequence: 2 givenname: Scott surname: Dorland fullname: Dorland, Scott organization: Division of Molecular Biology and Genetics, Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah Health Sciences Center – sequence: 3 givenname: David J. surname: Stillman fullname: Stillman, David J. email: stillman@genetics.utah.edu organization: Division of Molecular Biology and Genetics, Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah Health Sciences Center |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9234741$$D View this record in MEDLINE/PubMed |
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Mendeley... The SIN3 gene is required for the transcriptional repression of diverse genes in Saccharomyces cerevisiae. Sin3p does not bind directly to DNA but is thought... |
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SubjectTerms | Bacterial Proteins - genetics Chromatography, Gel - methods Fungal Proteins - analysis Fungal Proteins - metabolism Genes, Fungal Histone Deacetylases Macromolecular Substances Molecular Weight Multiprotein Complexes Recombinant Fusion Proteins Repressor Proteins - analysis Repressor Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae Proteins Serine Endopeptidases - genetics Transcription Factors - analysis Transcription Factors - metabolism Transcription, Genetic |
Title | A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators |
URI | http://mcb.asm.org/content/17/8/4852.abstract https://www.tandfonline.com/doi/abs/10.1128/MCB.17.8.4852 https://www.ncbi.nlm.nih.gov/pubmed/9234741 https://search.proquest.com/docview/16055789 https://search.proquest.com/docview/79155561 https://pubmed.ncbi.nlm.nih.gov/PMC232337 |
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