Ontology highlight
ABSTRACT:
SUBMITTER: Morris SA
PROVIDER: S-EPMC2811852 | biostudies-literature | 2007 Mar
REPOSITORIES: biostudies-literature
Morris Stephanie A SA Rao Bhargavi B Garcia Benjamin A BA Hake Sandra B SB Diaz Robert L RL Shabanowitz Jeffrey J Hunt Donald F DF Allis C David CD Lieb Jason D JD Strahl Brian D BD
The Journal of biological chemistry 20061221 10
Histone lysine 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 analyses of H3 purified from Tetrahymena thermophila and Saccharomyces cerevisiae (yeast), we find that H3K36 can be acetylated or methylated. Using an antibody specific to H3K36ac, we show that this modification is conserved in mammals. ...[more]