Site-specific ubiquitylation acts as a regulator of linker histone H1.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
09 06 2021
09 06 2021
Historique:
received:
12
09
2020
accepted:
03
05
2021
entrez:
10
6
2021
pubmed:
11
6
2021
medline:
23
6
2021
Statut:
epublish
Résumé
Decoding the role of histone posttranslational modifications (PTMs) is key to understand the fundamental process of epigenetic regulation. This is well studied for PTMs of core histones but not for linker histone H1 in general and its ubiquitylation in particular due to a lack of proper tools. Here, we report on the chemical synthesis of site-specifically mono-ubiquitylated H1.2 and identify its ubiquitin-dependent interactome on a proteome-wide scale. We show that site-specific ubiquitylation of H1 at position K64 modulates interactions with deubiquitylating enzymes and the deacetylase SIRT1. Moreover, it affects H1-dependent chromatosome assembly and phase separation resulting in a more open chromatosome conformation generally associated with a transcriptionally active chromatin state. In summary, we propose that site-specific ubiquitylation plays a general regulatory role for linker histone H1.
Identifiants
pubmed: 34108453
doi: 10.1038/s41467-021-23636-5
pii: 10.1038/s41467-021-23636-5
pmc: PMC8190259
doi:
Substances chimiques
Chromatin
0
H1-2 protein, human
0
Histones
0
Nucleosomes
0
Ubiquitin
0
Deubiquitinating Enzymes
EC 3.4.19.12
SIRT1 protein, human
EC 3.5.1.-
Sirtuin 1
EC 3.5.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3497Références
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