Histone Octamer Structure Is Altered Early in ISW2 ATP-Dependent Nucleosome Remodeling.
Adenosine Triphosphatases
/ genetics
Adenosine Triphosphate
/ metabolism
Catalytic Domain
/ genetics
Chromatin Assembly and Disassembly
/ genetics
Computer Simulation
DNA Footprinting
Histones
/ chemistry
Mass Spectrometry
Models, Molecular
Nucleosomes
/ chemistry
Protein Binding
Saccharomyces cerevisiae
/ genetics
Transcription Factors
/ genetics
ISWI
SANT domain
chromatin remodeling
gene regulation
histones
nucleosome dynamics
nucleosome movement
nucleosome structure
transcription
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
02 07 2019
02 07 2019
Historique:
received:
29
11
2017
revised:
24
04
2019
accepted:
29
05
2019
entrez:
4
7
2019
pubmed:
4
7
2019
medline:
28
8
2020
Statut:
ppublish
Résumé
Nucleosomes are the fundamental building blocks of chromatin that regulate DNA access and are composed of histone octamers. ATP-dependent chromatin remodelers like ISW2 regulate chromatin access by translationally moving nucleosomes to different DNA regions. We find that histone octamers are more pliable than previously assumed and distorted by ISW2 early in remodeling before DNA enters nucleosomes and the ATPase motor moves processively on nucleosomal DNA. Uncoupling the ATPase activity of ISW2 from nucleosome movement with deletion of the SANT domain from the C terminus of the Isw2 catalytic subunit traps remodeling intermediates in which the histone octamer structure is changed. We find restricting histone movement by chemical crosslinking also traps remodeling intermediates resembling those seen early in ISW2 remodeling with loss of the SANT domain. Other evidence shows histone octamers are intrinsically prone to changing their conformation and can be distorted merely by H3-H4 tetramer disulfide crosslinking.
Identifiants
pubmed: 31269447
pii: S2211-1247(19)30745-4
doi: 10.1016/j.celrep.2019.05.106
pii:
doi:
Substances chimiques
Histones
0
ISWI protein
0
Nucleosomes
0
Transcription Factors
0
Adenosine Triphosphate
8L70Q75FXE
Adenosine Triphosphatases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, N.I.H., Intramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
282-294.e6Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM110064
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL133678
Pays : United States
Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.