A Read/Write Mechanism Connects p300 Bromodomain Function to H2A.Z Acetylation.
Biochemistry
Biological Sciences
Cell Biology
Molecular Biology
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
22 Nov 2019
22 Nov 2019
Historique:
received:
22
03
2019
revised:
20
09
2019
accepted:
24
10
2019
pubmed:
16
11
2019
medline:
16
11
2019
entrez:
16
11
2019
Statut:
ppublish
Résumé
Acetylation of the histone variant H2A.Z (H2A.Zac) occurs at active regulatory regions associated with gene expression. Although the Tip60 complex is proposed to acetylate H2A.Z, functional studies suggest additional enzymes are involved. Here, we show that p300 acetylates H2A.Z at multiple lysines. In contrast, we found that although Tip60 does not efficiently acetylate H2A.Z in vitro, genetic inhibition of Tip60 reduces H2A.Zac in cells. Importantly, we found that interaction between the p300-bromodomain and H4 acetylation (H4ac) enhances p300-driven H2A.Zac. Indeed, H2A.Zac and H4ac show high genomic overlap, especially at active promoters. We also reveal unique chromatin features and transcriptional states at enhancers correlating with co-occurrence or exclusivity of H4ac and H2A.Zac. We propose that differential H4 and H2A.Z acetylation signatures can also define the enhancer state. In conclusion, we show both Tip60 and p300 contribute to H2A.Zac and reveal molecular mechanisms of writer/reader crosstalk between H2A.Z and H4 acetylation through p300.
Identifiants
pubmed: 31727574
pii: S2589-0042(19)30434-1
doi: 10.1016/j.isci.2019.10.053
pmc: PMC6889796
pii:
doi:
Types de publication
Journal Article
Langues
eng
Pagination
773-788Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM124736
Pays : United States
Informations de copyright
Copyright © 2019 The Author(s). Published by Elsevier Inc. All rights reserved.
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