ArticlePLoS biology2008
Reconstitution of DNA strand exchange mediated by Rhp51 recombinase and two mediators.
Article in PLoS biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 66 citations in OpenAlex.
- 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
- The Swi5-Sfr1 complex regulates Dmc1- and Rad51-driven DNA strand exchange proceeding through two distinct three-stranded intermediates by different mechanisms.Nucleic acids research · 2024Article
- Hop2-Mnd1 and Swi5-Sfr1 stimulate Dmc1 filament assembly using distinct mechanisms.Nucleic acids research · 2023Article
- Fission yeast Swi2 designates cell-type specific donor and stimulates Rad51-driven strand exchange for mating-type switching.Nucleic acids research · 2023Article
- The Fission Yeast Mating-Type Switching Motto: "One-for-Two" and "Two-for-One".Microbiology and molecular biology reviews : MMBR · 2023Review
- Genetic interaction of the histone chaperonemicroPublication biology · 2022Article
- How strand exchange protein function benefits from ATP hydrolysis.Current opinion in genetics & development · 2021Review
- Rrp1 translocase and ubiquitin ligase activities restrict the genome destabilising effects of Rad51 in fission yeast.Nucleic acids research · 2021Article
- A novel motif of Rad51 serves as an interaction hub for recombination auxiliary factors.eLife · 2021Article
- 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
- Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex.eLife · 2020Article
- Mating-type switching by homology-directed recombinational repair: a matter of choice.Current genetics · 2019Review
- Combination of coarse-grained molecular dynamics simulations and small-angle X-ray scattering experiments.Biophysics and physicobiology · 2019Article
- Topological DNA-binding of structural maintenance of chromosomes-like RecN promotes DNA double-strand break repair inCommunications biology · 2019Article
- 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
- New insights into donor directionality of mating-type switching in Schizosaccharomyces pombe.PLoS genetics · 2018Article
- Article
- Lingering single-strand breaks trigger Rad51-independent homology-directed repair of collapsed replication forks in the polynucleotide kinase/phosphatase mutant of fission yeast.PLoS genetics · 2017Article
- Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the fission yeast Schizosaccharomyces pombe, genetic evidence suggests that two mediators, Rad22 (the S. pombe Rad52 homolog) and the Swi5-Sfr1 complex, participate in a common pathway of Rhp51 (the S. pombe Rad51 homolog)-mediated homologous recombination (HR) and HR repair. Here, we have demonstrated an in vitro reconstitution of the central step of DNA strand exchange during HR. Our system consists entirely of homogeneously purified proteins, including Rhp51, the two mediators, and replication protein A (RPA), which reflects genetic requirements in vivo. Using this system, we present the first robust biochemical evidence that concerted action of the two mediators directs the loading of Rhp51 onto single-stranded DNA (ssDNA) precoated with RPA. Dissection of the reaction reveals that Rad22 overcomes the inhibitory effect of RPA on Rhp51-Swi5-Sfr1-mediated strand exchange. In addition, Rad22 negates the requirement for a strict order of protein addition to the in vitro system. However, despite the presence of Rad22, Swi5-Sfr1 is still essential for strand exchange. Importantly, Rhp51, but neither Rad22 nor the Swi5-Sfr1 mediator, is the factor that displaces RPA from ssDNA. Swi5-Sfr1 stabilizes Rhp51-ssDNA filaments in an ATP-dependent manner, and this stabilization is correlated with activation of Rhp51 for the strand exchange reaction. Rad22 alone cannot activate the Rhp51 presynaptic filament. AMP-PNP, a nonhydrolyzable ATP analog, induces a similar stabilization of Rhp51, but this stabilization is independent of Swi5-Sfr1. However, hydrolysis of ATP is required for processive strand transfer, which results in the formation of a long heteroduplex. Our in vitro reconstitution system has revealed that the two mediators have indispensable, but distinct, roles for mediating Rhp51 loading onto RPA-precoated ssDNA.
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