Schizosaccharomyces pombe KAT5 contributes to resection and repair of a DNA double-strand break.
Chromatin
/ metabolism
Chromatin Assembly and Disassembly
Chromosomes, Fungal
/ metabolism
DNA Breaks, Double-Stranded
DNA Repair
DNA, Fungal
/ genetics
Endodeoxyribonucleases
/ genetics
Histone Acetyltransferases
/ genetics
Histones
/ metabolism
Homologous Recombination
Lysine Acetyltransferase 5
/ genetics
Schizosaccharomyces
/ genetics
Schizosaccharomyces pombe Proteins
/ genetics
DSB repair
KAT5
Mst1
fission yeast
resection
Journal
Genetics
ISSN: 1943-2631
Titre abrégé: Genetics
Pays: United States
ID NLM: 0374636
Informations de publication
Date de publication:
17 05 2021
17 05 2021
Historique:
received:
02
02
2021
accepted:
04
03
2021
pubmed:
17
3
2021
medline:
19
2
2022
entrez:
16
3
2021
Statut:
ppublish
Résumé
Chromatin remodeling is essential for effective repair of a DNA double-strand break (DSB). KAT5 (Schizosaccharomyces pombe Mst1, human TIP60) is a MYST family histone acetyltransferase conserved from yeast to humans that coordinates various DNA damage response activities at a DNA DSB, including histone remodeling and activation of the DNA damage checkpoint. In S. pombe, mutations in mst1+ causes sensitivity to DNA damaging drugs. Here we show that Mst1 is recruited to DSBs. Mutation of mst1+ disrupts recruitment of repair proteins and delays resection. These defects are partially rescued by deletion of pku70, which has been previously shown to antagonize repair by homologous recombination (HR). These phenotypes of mst1 are similar to pht1-4KR, a nonacetylatable form of histone variant H2A.Z, which has been proposed to affect resection. Our data suggest that Mst1 functions to direct repair of DSBs toward HR pathways by modulating resection at the DSB.
Identifiants
pubmed: 33723569
pii: 6173406
doi: 10.1093/genetics/iyab042
pmc: PMC8128414
pii:
doi:
Substances chimiques
Chromatin
0
DNA, Fungal
0
Histones
0
Schizosaccharomyces pombe Proteins
0
Histone Acetyltransferases
EC 2.3.1.48
Lysine Acetyltransferase 5
EC 2.3.1.48
Endodeoxyribonucleases
EC 3.1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM118109
Pays : United States
Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Genetics Society of America. All rights reserved. For permissions, please email: journals.permissions@oup.com.
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