Conservation and divergence of meiotic DNA double strand break forming mechanisms in Arabidopsis thaliana.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
27 09 2021
27 09 2021
Historique:
accepted:
04
08
2021
revised:
16
07
2021
received:
01
02
2021
pubmed:
31
8
2021
medline:
17
12
2021
entrez:
30
8
2021
Statut:
ppublish
Résumé
In the current meiotic recombination initiation model, the SPO11 catalytic subunits associate with MTOPVIB to form a Topoisomerase VI-like complex that generates DNA double strand breaks (DSBs). Four additional proteins, PRD1/AtMEI1, PRD2/AtMEI4, PRD3/AtMER2 and the plant specific DFO are required for meiotic DSB formation. Here we show that (i) MTOPVIB and PRD1 provide the link between the catalytic sub-complex and the other DSB proteins, (ii) PRD3/AtMER2, while localized to the axis, does not assemble a canonical pre-DSB complex but establishes a direct link between the DSB-forming and resection machineries, (iii) DFO controls MTOPVIB foci formation and is part of a divergent RMM-like complex including PHS1/AtREC114 and PRD2/AtMEI4 but not PRD3/AtMER2, (iv) PHS1/AtREC114 is absolutely unnecessary for DSB formation despite having a conserved position within the DSB protein network and (v) MTOPVIB and PRD2/AtMEI4 interact directly with chromosome axis proteins to anchor the meiotic DSB machinery to the axis.
Identifiants
pubmed: 34458909
pii: 6357737
doi: 10.1093/nar/gkab715
pmc: PMC8464057
doi:
Substances chimiques
ASY1 protein, Arabidopsis
0
ASY3 protein, Arabidopsis
0
Arabidopsis Proteins
0
Cell Cycle Proteins
0
Chromatin
0
DFO protein, Arabidopsis
0
DNA-Binding Proteins
0
Spo11-1 protein, Arabidopsis
0
PHS1 protein, Arabidopsis
EC 3.1.3.48
Protein Tyrosine Phosphatases
EC 3.1.3.48
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
9821-9835Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.
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