Chromatin condensation fluctuations rather than steady-state predict chromatin accessibility.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
09 07 2019
09 07 2019
Historique:
accepted:
07
05
2019
revised:
24
04
2019
received:
18
01
2019
pubmed:
14
5
2019
medline:
26
2
2020
entrez:
14
5
2019
Statut:
ppublish
Résumé
Chromatin accessibility to protein factors is critical for genome activities. However, the dynamic properties of chromatin higher-order structures that regulate its accessibility are poorly understood. Here, we took advantage of the microenvironment sensitivity of the fluorescence lifetime of EGFP-H4 histone incorporated in chromatin to map in the nucleus of live cells the dynamics of chromatin condensation and its direct interaction with a tail acetylation recognition domain (the double bromodomain module of human TAFII250, dBD). We reveal chromatin condensation fluctuations supported by mechanisms fundamentally distinct from that of condensation. Fluctuations are spontaneous, yet their amplitudes are affected by their sub-nuclear localization and by distinct and competing mechanisms dependent on histone acetylation, ATP and both. Moreover, we show that accessibility of acetylated histone H4 to dBD is not restricted by chromatin condensation nor predicted by acetylation, rather, it is predicted by chromatin condensation fluctuations.
Identifiants
pubmed: 31081027
pii: 5488532
doi: 10.1093/nar/gkz373
pmc: PMC6614833
doi:
Substances chimiques
Chromatin
0
Fluorescent Dyes
0
Histones
0
TATA-Binding Protein Associated Factors
0
enhanced green fluorescent protein
0
Green Fluorescent Proteins
147336-22-9
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6184-6194Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.
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