A Histone Acetylation Switch Regulates H2A.Z Deposition by the SWR-C Remodeling Enzyme

Author:

Watanabe Shinya1,Radman-Livaja Marta2,Rando Oliver J.2,Peterson Craig L.1

Affiliation:

1. Program in Molecular Medicine, 373 Plantation Street, University of Massachusetts Medical School, Worcester, MA 01605, USA.

2. Department of Biochemistry and Molecular Pharmacology, 364 Plantation Street, University of Massachusetts Medical School, Worcester, MA 01605, USA.

Abstract

Variants and Regulation Genomic DNA is packaged into nucleosomes by spooling around histone proteins. Histone variants and the composition of nucleosomes can influence gene expression, as well as other chromatin-mediated processes. For example, the H2A.Z histone variant flanks RNA polII promoters, and such nucleosomes show rapid turnover, as well as enrichment for histone H3 acetylated at lysine 56 (H3-K56Ac). Watanabe et al. (p. 195 ) show that H3-K56Ac alters the substrate specificity of the chromatin remodeling enzyme SWR-C, which normally evicts nucleosomal H2A.Z such that it now rapidly exchanges both canonical H2A and the variant H2A.Z, modulating nucleosome turnover and therefore influencing gene regulation. Pathways are dramatically simplified, promoting proper folding.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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