ArticleNucleic acids research2024
DMC1 and RAD51 bind FxxA and FxPP motifs of BRCA2 via two separate interfaces.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Mechanisms That Govern Recombinase Fidelity Control During Eukaryotic Homologous Recombination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Structures and molecular mechanisms of RAD54B in modulating homologous recombination.bioRxiv : the preprint server for biology · 2026Article
- Modelling DMC1 mediated homologous recombination repair in mouse embryonic stem cells.Frontiers in cell and developmental biology · 2026Article
- Computationally-designed aptamers targeting RAD51-BRCA2 interaction impair homologous recombination and induce synthetic lethality.Nature communications · 2025Article
- Identification of missense DMC1 variants in males with non-obstructive azoospermia.Journal of assisted reproduction and genetics · 2025Article
- Moss BRCA2 lacking the canonical DNA-binding domain promotes homologous recombination and binds to DNA.Nucleic acids research · 2025Article
- Mechanism of Rad51 filament formation by Rad52 and Rad55-Rad57 in homologous recombination.Nature communications · 2025Article
- In silico structural analysis of Oryza sativa RAD51 reveals key interactions for nucleoprotein filament assembly and regulation.PloS one · 2025Article
- Rad52 sorts and stacks Rad51 at the DNA junction to promote homologous recombination.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
9 authors.
Funding
Abstract
In vertebrates, the BRCA2 protein is essential for meiotic and somatic homologous recombination due to its interaction with the RAD51 and DMC1 recombinases through FxxA and FxPP motifs (here named A- and P-motifs, respectively). The A-motifs present in the eight BRC repeats of BRCA2 compete with the A-motif of RAD51, which is responsible for its self-oligomerization. BRCs thus disrupt RAD51 nucleoprotein filaments in vitro. The role of the P-motifs is less studied. We recently found that deletion of Brca2 exons 12-14 encoding one of them (the prototypical 'PhePP' motif), disrupts DMC1 but not RAD51 function in mouse meiosis. Here we provide a mechanistic explanation for this phenotype by solving the crystal structure of the complex between a BRCA2 fragment containing the PhePP motif and DMC1. Our structure reveals that, despite sharing a conserved phenylalanine, the A- and P-motifs bind to distinct sites on the ATPase domain of the recombinases. The P-motif interacts with a site that is accessible in DMC1 octamers and nucleoprotein filaments. Moreover, we show that this interaction also involves the adjacent protomer and thus increases the stability of the DMC1 nucleoprotein filaments. We extend our analysis to other P-motifs from RAD51AP1 and FIGNL1.
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