A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators

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Published inMolecular and Cellular Biology Vol. 17; no. 8; pp. 4852 - 4858
Main Authors Kasten, Margaret M., Dorland, Scott, Stillman, David J.
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.08.1997
Taylor & Francis
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Abstract 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       
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.
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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
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  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
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  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
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  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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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
Volume 17
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