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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-11-6
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pubmed:abstractText |
The functions of the SAGA and SWI/SNF complexes are interrelated and can form stable "epigenetic marks" on promoters in vivo. Here we show that stable promoter occupancy by SWI/SNF and SAGA in the absence of transcription activators requires the bromodomains of the Swi2/Snf2 and Gcn5 subunits, respectively, and nucleosome acetylation. This acetylation can be brought about by either the SAGA or NuA4 HAT complexes. The bromodomain in the Spt7 subunit of SAGA is dispensable for this activity but will anchor SAGA if it is swapped into Gcn5, indicating that specificity of bromodomain function is determined in part by the subunit it occupies. Thus, bromodomains within the catalytic subunits of SAGA and SWI/SNF anchor these complexes to acetylated promoter nucleosomes.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GCN5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Gal-VP16,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/SPT7 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
111
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
369-79
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12419247-Acetylation,
pubmed-meshheading:12419247-Acetyltransferases,
pubmed-meshheading:12419247-Chromatin,
pubmed-meshheading:12419247-DNA-Binding Proteins,
pubmed-meshheading:12419247-Histone Acetyltransferases,
pubmed-meshheading:12419247-Nuclear Proteins,
pubmed-meshheading:12419247-Nucleosomes,
pubmed-meshheading:12419247-Promoter Regions, Genetic,
pubmed-meshheading:12419247-Protein Kinases,
pubmed-meshheading:12419247-Protein Structure, Tertiary,
pubmed-meshheading:12419247-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12419247-Trans-Activators,
pubmed-meshheading:12419247-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 306 Althouse Laboratory, University Park, PA 16802, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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