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Data from: Diverse nucleosome site-selectivity among histone deacetylase complexes

Citation

Wang, Zhipeng et al. (2020), Data from: Diverse nucleosome site-selectivity among histone deacetylase complexes, Dryad, Dataset, https://doi.org/10.5061/dryad.x0k6djhgc

Abstract

Histone acetylation regulates chromatin structure and gene expression and is removed by histone deacetylases (HDACs). HDACs are commonly found in various protein complexes to confer distinct cellular functions, but how the multi-subunit complexes influence deacetylase activities and site-selectivities in chromatin is poorly understood. Recent studies on the HDAC1 containing CoREST complex and acetylated nucleosome substrates revealed a notable preference for deacetylation of histone H3 acetyl-Lys9 vs. acetyl-Lys14 (M. Wu et al, 2018). Here we analyze the enzymatic properties of five class I HDAC complexes: CoREST, NuRD, Sin3B, MiDAC and SMRT with site-specific acetylated nucleosome substrates. Our results demonstrate that these HDAC complexes show a wide variety of deacetylase rates in a site-selective manner. A Gly13 in the histone H3 tail is responsible for a sharp reduction in deacetylase activity of the CoREST complex for H3K14ac. These studies provide a framework for connecting enzymatic and biological functions of specific HDAC complexes.

Funding

National Institutes of Health, Award: GM64237

Leukemia and Lymphoma Society, Award: SCOR

Wellcome Trust Senior Investigator Award, Award: 100237/Z/12/Z

Wellcome Trust Senior Investigator Award, Award: 100237/Z/12/Z