Diverse nucleosome Site-Selectivity among histone deacetylase complexes.
CoREST
HDAC
biochemistry
chemical biology
enzyme
histone
human
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
05 06 2020
05 06 2020
Historique:
received:
09
04
2020
accepted:
04
06
2020
pubmed:
6
6
2020
medline:
19
3
2021
entrez:
6
6
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32501215
doi: 10.7554/eLife.57663
pii: 57663
pmc: PMC7316510
doi:
pii:
Substances chimiques
Co-Repressor Proteins
0
Histones
0
Nerve Tissue Proteins
0
Nucleosomes
0
RCOR1 protein, human
0
Histone Deacetylases
EC 3.5.1.98
Mi-2 Nucleosome Remodeling and Deacetylase Complex
EC 3.5.1.98
Banques de données
Dryad
['10.5061/dryad.x0k6djhgc']
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : R37 GM062437
Pays : United States
Organisme : Wellcome Trust Senior Investigator Award
ID : 100237/Z/12/Z
Pays : International
Organisme : NIH HHS
ID : GM62437
Pays : United States
Informations de copyright
© 2020, Wang et al.
Déclaration de conflit d'intérêts
ZW, CM, CL, JG, MW, KL, LF, JS No competing interests declared, PC Senior editor, eLife
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