Rif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
10 06 2019
10 06 2019
Historique:
received:
22
08
2018
accepted:
08
05
2019
entrez:
12
6
2019
pubmed:
12
6
2019
medline:
5
7
2019
Statut:
epublish
Résumé
Rif1 is involved in telomere homeostasis, DNA replication timing, and DNA double-strand break (DSB) repair pathway choice from yeast to human. The molecular mechanisms that enable Rif1 to fulfill its diverse roles remain to be determined. Here, we demonstrate that Rif1 is S-acylated within its conserved N-terminal domain at cysteine residues C466 and C473 by the DHHC family palmitoyl acyltransferase Pfa4. Rif1 S-acylation facilitates the accumulation of Rif1 at DSBs, the attenuation of DNA end-resection, and DSB repair by non-homologous end-joining (NHEJ). These findings identify S-acylation as a posttranslational modification regulating DNA repair. S-acylated Rif1 mounts a localized DNA-damage response proximal to the inner nuclear membrane, revealing a mechanism of compartmentalized DSB repair pathway choice by sequestration of a fatty acylated repair factor at the inner nuclear membrane.
Identifiants
pubmed: 31182712
doi: 10.1038/s41467-019-10349-z
pii: 10.1038/s41467-019-10349-z
pmc: PMC6557901
doi:
Substances chimiques
Repressor Proteins
0
Saccharomyces cerevisiae Proteins
0
Telomere-Binding Proteins
0
RIF1 protein, S cerevisiae
146589-82-4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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