ArticleProceedings of the National Academy of Sciences of the United States of America2018
Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Nucleostemin promotes RAD51 filament assembly on double-stranded DNA to protect stalled replication forks.Nucleic acids research · 2026Article
- Mei5-Sae3 stabilizes both active and inactive forms of Dmc1 filaments independently of its impact on ATP hydrolysis.Nucleic acids research · 2025Article
- SWI5-SFR1 reduces RAD51 recombinase extending units during filament assembly.Nucleic acids research · 2025Article
- Mei5-Sae3 stabilizes Dmc1 nucleating clusters for efficient Dmc1 assembly on RPA-coated single-stranded DNA.Nucleic acids research · 2024Article
- Hop2-Mnd1 and Swi5-Sfr1 stimulate Dmc1 filament assembly using distinct mechanisms.Nucleic acids research · 2023Article
- Rad52's DNA annealing activity drives template switching associated with restarted DNA replication.Nature communications · 2022Article
- Crosstalk between CST and RPA regulates RAD51 activity during replication stress.Nature communications · 2021Article
- The regulation mechanism of the C-terminus of RecA proteins during DNA strand-exchange process.Biophysical journal · 2021Article
- DNA Repair Pathway Choices in CRISPR-Cas9-Mediated Genome Editing.Trends in genetics : TIG · 2021Review
- A novel motif of Rad51 serves as an interaction hub for recombination auxiliary factors.eLife · 2021Article
- Identification of fidelity-governing factors in human recombinases DMC1 and RAD51 from cryo-EM structures.Nature communications · 2021Article
- Single-Molecule Tethered Particle Motion Studies on the DNA Recombinase Filament Assembly and Disassembly.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Microcephaly family protein MCPH1 stabilizes RAD51 filaments.Nucleic acids research · 2020Article
- Influence of the C-Terminal Tail of RecA Proteins from Alkaline pH-Resistant BacteriumACS omega · 2020Article
- Real-time tracking reveals catalytic roles for the two DNA binding sites of Rad51.Nature communications · 2020Article
- Two auxiliary factors promote Dmc1-driven DNA strand exchange via stepwise mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Rad51 facilitates filament assembly of meiosis-specific Dmc1 recombinase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex.eLife · 2020Article
- Homologous Recombination under the Single-Molecule Fluorescence Microscope.International journal of molecular sciences · 2019Review
- A mutant form of Dmc1 that bypasses the requirement for accessory protein Mei5-Sae3 reveals independent activities of Mei5-Sae3 and Rad51 in Dmc1 filament stability.PLoS genetics · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic Rad51 protein is essential for homologous-recombination repair of DNA double-strand breaks. Rad51 recombinases first assemble onto single-stranded DNA to form a nucleoprotein filament, required for function in homology pairing and strand exchange. This filament assembly is the first regulation step in homologous recombination. Rad51 nucleation is kinetically slow, and several accessory factors have been identified to regulate this step. Swi5-Sfr1 (S5S1) stimulates Rad51-mediated homologous recombination by stabilizing Rad51 nucleoprotein filaments, but the mechanism of stabilization is unclear. We used single-molecule tethered particle motion experiments to show that mouse S5S1 (mS5S1) efficiently stimulates mouse RAD51 (mRAD51) nucleus formation and inhibits mRAD51 dissociation from filaments. We also used single-molecule fluorescence resonance energy transfer experiments to show that mS5S1 promotes stable nucleus formation by specifically preventing mRAD51 dissociation. This leads to a reduction of nucleation size from three mRAD51 to two mRAD51 molecules in the presence of mS5S1. Compared with mRAD51, fission yeast Rad51 (SpRad51) exhibits fast nucleation but quickly dissociates from the filament. SpS5S1 specifically reduces SpRad51 disassembly to maintain a stable filament. These results clearly demonstrate the conserved function of S5S1 by primarily stabilizing Rad51 on DNA, allowing both the formation of the stable nucleus and the maintenance of filament length.
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