ArticleNature communications2013
Srs2 prevents Rad51 filament formation by repetitive motion on DNA.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
70 citing papers in PubMed, 103 citations in OpenAlex.
- A conserved mechanism for dimerization and activation of superfamily 1A UvrD-family helicases.Nucleic acids research · 2026Article
- Potential Rad54 separation of function mutation highlights unique roles during homologous recombination.PLoS genetics · 2026Article
- A conundrum resolved: regulation and activation of UvrD-family DNA helicases/translocases.Trends in biochemical sciences · 2026Review
- SRS2 is required for MUS81-dependent CO formation in zmm mutants.PLoS genetics · 2025Article
- Mechanism of Rad51 filament formation by Rad52 and Rad55-Rad57 in homologous recombination.Nature communications · 2025Article
- Deep structure-function analysis of the endonuclease Mus81 with dominant mutational scanning.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Rad52 sorts and stacks Rad51 at the DNA junction to promote homologous recombination.bioRxiv : the preprint server for biology · 2024Article
- The human Shu complex promotes RAD51 activity by modulating RPA dynamics on ssDNA.Nature communications · 2024Article
- The translocation activity of Rad54 reduces crossover outcomes during homologous recombination.Nucleic acids research · 2024Article
- All who wander are not lost: the search for homology during homologous recombination.Biochemical Society transactions · 2024Article
- The separation pin distinguishes the pro- and anti-recombinogenic functions of Saccharomyces cerevisiae Srs2.Nature communications · 2023Article
- Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.bioRxiv : the preprint server for biology · 2023Article
- ssDNA accessibility of Rad51 is regulated by orchestrating multiple RPA dynamics.Nature communications · 2023Article
- Article
- Single-molecule visualization of Pif1 helicase translocation on single-stranded DNA.The Journal of biological chemistry · 2023Article
- Article
- Bloom helicase mediates formation of large single-stranded DNA loops during DNA end processing.Nature communications · 2022Article
- Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022Review
- Rad54 and Rdh54 prevent Srs2-mediated disruption of Rad51 presynaptic filaments.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Next generation single-molecule techniques: Imaging, labeling, and manipulation in vitro and in cellulo.Molecular cell · 2022Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Srs2 dismantles presynaptic Rad51 filaments and prevents its re-formation as an anti-recombinase. However, the molecular mechanism by which Srs2 accomplishes these tasks remains unclear. Here we report a single-molecule fluorescence study of the dynamics of Rad51 filament formation and its disruption by Srs2. Rad51 forms filaments on single-stranded DNA by sequential binding of primarily monomers and dimers in a 5'-3' direction. One Rad51 molecule binds to three nucleotides, and six monomers are required to achieve a stable nucleation cluster. Srs2 exhibits ATP-dependent repetitive motion on single-stranded DNA and this activity prevents re-formation of the Rad51 filament. The same activity of Srs2 cannot prevent RecA filament formation, indicating its specificity for Rad51. Srs2's DNA-unwinding activity is greatly suppressed when Rad51 filaments form on duplex DNA. Taken together, our results reveal an exquisite and highly specific mechanism by which Srs2 regulates the Rad51 filament formation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.