Diverse nucleosome Site-Selectivity among histone deacetylase complexes

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-selectiviti...

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Published in:eLife 2020-06, Vol.9
Main Authors: Wang, Zhipeng A, Millard, Christopher J, Lin, Chia-Liang, Gurnett, Jennifer E, Wu, Mingxuan, Lee, Kwangwoon, Fairall, Louise, Schwabe, John Wr, Cole, Philip A
Format: Article
Language:English
Subjects:
Acetylation
Biochemistry and Chemical Biology
Chromatin
Chromatography
Co-Repressor Proteins - genetics
Co-Repressor Proteins - metabolism
CoREST
Deacetylation
Deoxyribonucleic acid
DNA
DNA methylation
enzyme
Enzymes
Gene expression
HDAC
histone
Histone deacetylase
Histone Deacetylases - genetics
Histone Deacetylases - metabolism
Histone H3
Histones - genetics
Histones - metabolism
Humans
Mi-2 Nucleosome Remodeling and Deacetylase Complex - genetics
Mi-2 Nucleosome Remodeling and Deacetylase Complex - metabolism
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Nucleosomes - genetics
Nucleosomes - metabolism
Peptides
Physiology
Proteins
Research Advance
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creator Wang, Zhipeng A
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Cole, Philip A
description 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. Previously we reported the results of studies on the HDAC1 containing CoREST complex and acetylated nucleosome substrates which revealed a notable preference for deacetylation of histone H3 acetyl-Lys9 vs. acetyl-Lys14 (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.
doi_str_mv 10.7554/elife.57663
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subjects Acetylation
Biochemistry and Chemical Biology
Chromatin
Chromatography
Co-Repressor Proteins - genetics
Co-Repressor Proteins - metabolism
CoREST
Deacetylation
Deoxyribonucleic acid
DNA
DNA methylation
enzyme
Enzymes
Gene expression
HDAC
histone
Histone deacetylase
Histone Deacetylases - genetics
Histone Deacetylases - metabolism
Histone H3
Histones - genetics
Histones - metabolism
Humans
Mi-2 Nucleosome Remodeling and Deacetylase Complex - genetics
Mi-2 Nucleosome Remodeling and Deacetylase Complex - metabolism
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Nucleosomes - genetics
Nucleosomes - metabolism
Peptides
Physiology
Proteins
Research Advance
title Diverse nucleosome Site-Selectivity among histone deacetylase complexes
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