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H3K36Ac ChIP chips

ABSTRACT: Histone lysine (K) acetylation is a major mechanism by which cells regulate the structure and function of chromatin, and new sites of acetylation continue to be discovered. Here we identify and characterize histone H3K36 acetylation (H3K36ac). By mass spectrometric analysis of H3 purified from Tetrahymena thermophila and S. cerevisiae (yeast), we find that H3K36 is acetylated in addition to being methylated. Using an antibody specific to H3K36ac, we show that this modification is conserved in mammals. In yeast, genome-wide ChIP-chip experiments show that H3K36ac is localized predominantly to the promoters of RNA polymerase II-transcribed genes, a pattern mutually exclusive to that of H3K36 methylation. The pattern of H3K36ac localization is similar to that of other sites of H3 acetylation, including H3K9ac and H3K14ac. Using histone acetyltransferase complexes purified from yeast, we show that the Gcn5-containing SAGA complex specifically acetylates H3K36 in vitro. Deletion of GCN5 completely abolishes H3K36ac in vivo. The regulation of H3K36ac by Gcn5 suggests a function for this modification in transcription. These data expand our knowledge of the genomic targets of Gcn5, show H3K36ac is highly conserved, and raise the intriguing possibility that the transition between H3K36ac and H3K36me acts as a switch in chromatin function along transcription units. This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE5544 | GEO | 2006/11/01

SECONDARY ACCESSION(S): PRJNA96033

REPOSITORIES: GEO

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