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dc.contributor.authorPollard, Kerri Jeanne
dc.contributor.authorPeterson, Craig L.
dc.date2022-08-11T08:09:03.000
dc.date.accessioned2022-08-23T16:16:30Z
dc.date.available2022-08-23T16:16:30Z
dc.date.issued1997-10-29
dc.date.submitted2008-11-26
dc.identifier.citation<p>Mol Cell Biol. 1997 Nov;17(11):6212-22.</p>
dc.identifier.issn0270-7306 (Print)
dc.identifier.doi10.1128/MCB.17.11.6212
dc.identifier.pmid9343382
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34347
dc.description.abstractThe Saccharomyces cerevisiae SWI/SNF complex is a 2-MDa multimeric assembly that facilitates transcriptional enhancement by antagonizing chromatin-mediated transcriptional repression. We show here that mutations in ADA2, ADA3, and GCN5, which are believed to encode subunits of a nuclear histone acetyltransferase complex, cause phenotypes strikingly similar to that of swi/snf mutants. ADA2, ADA3, and GCN5 are required for full expression of all SWI/SNF-dependent genes tested, including HO, SUC2, INO1, and Ty elements. Furthermore, mutations in the SIN1 gene, which encodes a nonhistone chromatin component, or mutations in histone H3 or H4 partially alleviate the transcriptional defects caused by ada/gcn5 or swi/snf mutations. We also find that ada2 swi1, ada3 swi1, and gcn5 swi1 double mutants are inviable and that mutations in SIN1 allow viability of these double mutants. We have partially purified three chromatographically distinct GCN5-dependent acetyltransferase activities, and we show that these enzymes can acetylate both histones and Sin1p. We propose a model in which the ADA/GCN5 and SWI/SNF complexes facilitate activator function by acting in concert to disrupt or modify chromatin structure.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9343382&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC232472/
dc.subjectAcetylation; Acetyltransferases; Chromatin; Chromosomal Proteins, Non-Histone; Cloning, Molecular; DNA-Binding Proteins; Fungal Proteins; *Gene Expression Regulation, Fungal; Genes, Fungal; Histone Acetyltransferases; Protein Binding; Protein Kinases; Repressor Proteins; Saccharomyces cerevisiae; *Saccharomyces cerevisiae Proteins; Sequence Analysis, DNA; Transcription Factors; *Transcription, Genetic
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleRole for ADA/GCN5 products in antagonizing chromatin-mediated transcriptional repression
dc.typeJournal Article
dc.source.journaltitleMolecular and cellular biology
dc.source.volume17
dc.source.issue11
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/994
dc.identifier.contextkey673210
html.description.abstract<p>The Saccharomyces cerevisiae SWI/SNF complex is a 2-MDa multimeric assembly that facilitates transcriptional enhancement by antagonizing chromatin-mediated transcriptional repression. We show here that mutations in ADA2, ADA3, and GCN5, which are believed to encode subunits of a nuclear histone acetyltransferase complex, cause phenotypes strikingly similar to that of swi/snf mutants. ADA2, ADA3, and GCN5 are required for full expression of all SWI/SNF-dependent genes tested, including HO, SUC2, INO1, and Ty elements. Furthermore, mutations in the SIN1 gene, which encodes a nonhistone chromatin component, or mutations in histone H3 or H4 partially alleviate the transcriptional defects caused by ada/gcn5 or swi/snf mutations. We also find that ada2 swi1, ada3 swi1, and gcn5 swi1 double mutants are inviable and that mutations in SIN1 allow viability of these double mutants. We have partially purified three chromatographically distinct GCN5-dependent acetyltransferase activities, and we show that these enzymes can acetylate both histones and Sin1p. We propose a model in which the ADA/GCN5 and SWI/SNF complexes facilitate activator function by acting in concert to disrupt or modify chromatin structure.</p>
dc.identifier.submissionpathgsbs_sp/994
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages6212-22


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