Eaf3 Chromodomain Interaction with Methylated H3-K36 Links Histone Deacetylation to Pol II Elongation
نویسندگان
چکیده
منابع مشابه
Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation.
Eaf3, a component of the NuA4 histone acetylase and Rpd3 histone deacetylase complexes, is important for the global pattern of histone acetylation in Saccharomyces cerevisiae. Preferential deacetylation of coding regions requires the Eaf3 chromodomain and H3-K36 methylation by Set2. The Eaf3 chromodomain interacts with methylated H3-K36 peptides, suggesting that this interaction leads to prefer...
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The yeast histone deacetylase Rpd3 can be recruited to promoters to repress transcription initiation. Biochemical, genetic, and gene-expression analyses show that Rpd3 exists in two distinct complexes. The smaller complex, Rpd3C(S), shares Sin3 and Ume1 with Rpd3C(L) but contains the unique subunits Rco1 and Eaf3. Rpd3C(S) mutants exhibit phenotypes remarkably similar to those of Set2, a histon...
متن کاملHistone H3 lysine 36 methylation antagonizes silencing in Saccharomyces cerevisiae independently of the Rpd3S histone deacetylase complex.
In yeast, methylation of histone H3 on lysine 36 (H3-K36) is catalyzed by the NSD1 leukemia oncoprotein homolog Set2. The histone deacetylase complex Rpd3S is recruited to chromatin via binding of the chromodomain protein Eaf3 to methylated H3-K36 to prevent erroneous transcription initiation. Here we identify a distinct function for H3-K36 methylation. We used random mutagenesis of histones H3...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 2005
ISSN: 1097-2765
DOI: 10.1016/j.molcel.2005.11.021