Ontology highlight
ABSTRACT:
SUBMITTER: Watanabe S
PROVIDER: S-EPMC3727404 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature
Watanabe Shinya S Radman-Livaja Marta M Rando Oliver J OJ Peterson Craig L CL
Science (New York, N.Y.) 20130401 6129
The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function. H2A.Z deposition is controlled by SWR-C chromatin remodeling enzymes that catalyze the nucleosomal exchange of canonical H2A with H2A.Z. Here we report that acetylation of histone H3 on lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange in which either H2A.Z or H2A can be exchanged from nucleosomes. This result was confirmed in vivo, where genome-w ...[more]