Linker histones and chromatin remodelling complexes maintain genome stability and control cellular ageing.
Actin-related protein 4
Chromatin remodelling
Chronological ageing
Linker histones
Saccharomyces cerevisiae
Journal
Mechanisms of ageing and development
ISSN: 1872-6216
Titre abrégé: Mech Ageing Dev
Pays: Ireland
ID NLM: 0347227
Informations de publication
Date de publication:
01 2019
01 2019
Historique:
received:
28
02
2018
revised:
06
07
2018
accepted:
12
07
2018
pubmed:
22
7
2018
medline:
25
4
2019
entrez:
21
7
2018
Statut:
ppublish
Résumé
Linker histones are major players in chromatin organization and per se are essential players in genome homeostasis. As the fifth class of histone proteins the linker histones not only interact with DNA and core histones but also with other chromatin proteins. These interactions prove to be essential for the higher levels of chromatin organization like chromatin loops, transcription factories and chromosome territories. Our recent results have proved that Saccharomyces cerevisiae linker histone - Hho1p, physically interacts with the actin-related protein 4 (Arp4) and that the abrogation of this interaction through the deletion of the gene for the linker histone in arp4 mutant cells leads to global changes in chromatin compaction. Here, we show that the healthy interaction between the yeast linker histone and Arp4p is critical for maintaining genome stability and for controlling cellular sensitivity to different types of stress. The abolished interaction between the linker histone and Arp4p leads the mutant yeast cells to premature ageing phenotypes. Cells die young and are more sensitive to stress. These results unambiguously prove the role of linker histones and chromatin remodelling in ageing by their cooperation in pertaining higher-order chromatin compaction and thus maintaining genome stability.
Identifiants
pubmed: 30025887
pii: S0047-6374(18)30051-4
doi: 10.1016/j.mad.2018.07.002
pii:
doi:
Substances chimiques
Actins
0
Arp4 protein, S cerevisiae
0
HHO1 protein, S cerevisiae
0
Histones
0
Nuclear Proteins
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
55-65Informations de copyright
Copyright © 2018 Elsevier B.V. All rights reserved.