The histone H3.1 variant regulates TONSOKU-mediated DNA repair during replication.
Arabidopsis
/ genetics
Arabidopsis Proteins
/ chemistry
DNA Breaks, Double-Stranded
DNA Repair
DNA Replication
DNA, Plant
/ metabolism
DNA-Directed DNA Polymerase
/ genetics
Genome, Plant
Genomic Instability
Histones
/ chemistry
Lysine
/ metabolism
Methylation
Methyltransferases
/ genetics
Mutation
Protein Interaction Domains and Motifs
DNA Polymerase theta
Journal
Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511
Informations de publication
Date de publication:
18 03 2022
18 03 2022
Historique:
entrez:
17
3
2022
pubmed:
18
3
2022
medline:
30
3
2022
Statut:
ppublish
Résumé
The tail of replication-dependent histone H3.1 varies from that of replication-independent H3.3 at the amino acid located at position 31 in plants and animals, but no function has been assigned to this residue to demonstrate a unique and conserved role for H3.1 during replication. We found that TONSOKU (TSK/TONSL), which rescues broken replication forks, specifically interacts with H3.1 via recognition of alanine 31 by its tetratricopeptide repeat domain. Our results indicate that genomic instability in the absence of ATXR5/ATXR6-catalyzed histone H3 lysine 27 monomethylation in plants depends on H3.1, TSK, and DNA polymerase theta (Pol θ). This work reveals an H3.1-specific function during replication and a common strategy used in multicellular eukaryotes for regulating post-replicative chromatin maturation and TSK, which relies on histone monomethyltransferases and reading of the H3.1 variant.
Identifiants
pubmed: 35298257
doi: 10.1126/science.abm5320
pmc: PMC9153895
mid: NIHMS1807518
doi:
Substances chimiques
Arabidopsis Proteins
0
DNA, Plant
0
Histones
0
ATXR5 protein, Arabidopsis
EC 2.1.1.-
ATXR6 protein, Arabidopsis
EC 2.1.1.-
Methyltransferases
EC 2.1.1.-
DNA-Directed DNA Polymerase
EC 2.7.7.7
Lysine
K3Z4F929H6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1281-1286Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM128661
Pays : United States
Commentaires et corrections
Type : CommentIn
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