Abstract
The positive link between the SWI/SNF and the Gcn5 histone acetyltransferase in transcriptional activation has been well described. Here we report an inhibitory role for Gcn5 in SWI/SNF targeting. We demonstrate that Gcn5-containing complexes directly acetylate the Snf2 subunit of the SWI/SNF complex in vitro, as well as in vivo. Moreover, the acetylation of Snf2 facilitates the dissociation of the SWI/SNF complex from acetylated histones, and reduces its association with promoters in vivo. These data reveal a novel mechanism by which Gcn5 modulates chromatin structure not only through the acetylation of histones, but also by directly acetylating Snf2.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation
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Adenosine Triphosphatases / metabolism*
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Chromatin / metabolism*
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Fungal Proteins / metabolism*
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Fungal Proteins / physiology
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Histone Acetyltransferases / physiology*
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Histones / metabolism
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Multiprotein Complexes / metabolism
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Promoter Regions, Genetic
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Protein Binding
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Saccharomyces cerevisiae Proteins / metabolism*
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Saccharomyces cerevisiae Proteins / physiology*
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Transcription Factors / metabolism*
Substances
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Chromatin
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Fungal Proteins
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Histones
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Multiprotein Complexes
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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GCN5 protein, S cerevisiae
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Histone Acetyltransferases
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Adenosine Triphosphatases
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SNF2 protein, S cerevisiae