E-GEOD-43935 - A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme

Released on 15 April 2013, last updated on 25 April 2013
Saccharomyces cerevisiae W303
Samples (3)
Protocols (4)
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 lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange where either H2A.Z or H2A can be exchanged from nucleosomes. This result is confirmed in vivo, where genome-wide analysis demonstrates widespread decreases in H2A.Z levels in yeast mutants with hyperacetylated H3K56. Our work also suggests that a conserved SWR-C subunit may function as a “lock” that prevents removal of H2A.Z from nucleosomes. Our study identifies a histone modification that regulates a chromatin remodeling reaction and provides insights into how histone variants and nucleosome turnover can be controlled by chromatin regulators. H2A.Z ChIP seq experiments in mutants with constitutive H3K56ac
Experiment type
Craig Petersen, Marta Radman-Livaja, Oliver Rando, Shinya Watanabe
Exp. designProtocolsVariablesProcessedSeq. reads
Investigation descriptionE-GEOD-43935.idf.txt
Sample and data relationshipE-GEOD-43935.sdrf.txt
Processed data (2)E-GEOD-43935.processed.1.zip, E-GEOD-43935.processed.2.zip