A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme.
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-wide analysis demonstrated 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.
Mesh Terms:
Acetylation, Adenosine Triphosphatases, Biocatalysis, Chromatin Assembly and Disassembly, Histones, Multienzyme Complexes, Nucleosomes, Protein Multimerization, Protein Stability, Protein Subunits, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity
Acetylation, Adenosine Triphosphatases, Biocatalysis, Chromatin Assembly and Disassembly, Histones, Multienzyme Complexes, Nucleosomes, Protein Multimerization, Protein Stability, Protein Subunits, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity
Science
Date: Apr. 12, 2013
PubMed ID: 23580526
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