ArticleNucleic acids research2016
Role of the RAD51-SWI5-SFR1 Ensemble in homologous recombination.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Whole exome sequencing reveals rare DNA repair gene variants in BRCA1/2-negative Arab early-onset breast cancer patients.Scientific reports · 2026Article
- RAD51 D-loop structures reveal the mechanism of eukaryotic RAD51-mediated strand exchange.Nature communications · 2025Article
- SWI5-SFR1 reduces RAD51 recombinase extending units during filament assembly.Nucleic acids research · 2025Article
- Engineering tripartite gene editing machinery for highly efficient non-viral targeted genome integration.Nature communications · 2025Article
- Multi-Level Control of the ATM/ATR-CHK1 Axis by the Transcription Factor E4F1 in Triple-Negative Breast Cancer.International journal of molecular sciences · 2022Article
- A novel motif of Rad51 serves as an interaction hub for recombination auxiliary factors.eLife · 2021Article
- Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex.eLife · 2020Article
- Guidelines for DNA recombination and repair studies: Mechanistic assays of DNA repair processes.Microbial cell (Graz, Austria) · 2019Review
- Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Review
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During DNA double-strand break and replication fork repair by homologous recombination, the RAD51 recombinase catalyzes the DNA strand exchange reaction via a helical polymer assembled on single-stranded DNA, termed the presynaptic filament. Our published work has demonstrated a dual function of the SWI5-SFR1 complex in RAD51-mediated DNA strand exchange, namely, by stabilizing the presynaptic filament and maintaining the catalytically active ATP-bound state of the filament via enhancement of ADP release. In this study, we have strived to determine the basis for physical and functional interactions between Mus musculus SWI5-SFR1 and RAD51. We found that SWI5-SFR1 preferentially associates with the oligomeric form of RAD51. Specifically, a C-terminal domain within SWI5 contributes to RAD51 interaction. With specific RAD51 interaction defective mutants of SWI5-SFR1 that we have isolated, we show that the physical interaction is indispensable for the stimulation of the recombinase activity of RAD51. Our results thus help establish the functional relevance of the trimeric RAD51-SWI5-SFR1 complex and provide insights into the mechanistic underpinnings of homology-directed DNA repair in mammalian cells.
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