ArticleGenetics2013
Remodeling of the Rad51 DNA strand-exchange protein by the Srs2 helicase.
Article in Genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Rad51, Rad54, and ZMM proteins antagonize the mismatch repair system to promote fertility of budding yeast intraspecies hybrid zygotes.Nucleic acids research · 2025Article
- SRS2 is required for MUS81-dependent CO formation in zmm mutants.PLoS genetics · 2025Article
- Recurrent DNA nicks drive massive expansions of (GAA)Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Replication protein-A, RPA, plays a pivotal role in the maintenance of recombination checkpoint in yeast meiosis.Scientific reports · 2024Article
- The separation pin distinguishes the pro- and anti-recombinogenic functions of Saccharomyces cerevisiae Srs2.Nature communications · 2023Article
- The Inability to Disassemble Rad51 Nucleoprotein Filaments Leads to Aberrant Mitosis and Cell Death.Biomedicines · 2023Article
- 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
- The Rad51 paralog complex Rad55-Rad57 acts as a molecular chaperone during homologous recombination.Molecular cell · 2021Article
- Single-molecule visualization of human RECQ5 interactions with single-stranded DNA recombination intermediates.Nucleic acids research · 2021Article
- A Rad51-independent pathway promotes single-strand template repair in gene editing.PLoS genetics · 2020Article
- Review
- 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
- S. cerevisiae Srs2 helicase ensures normal recombination intermediate metabolism during meiosis and prevents accumulation of Rad51 aggregates.Chromosoma · 2019Article
- Srs2 helicase prevents the formation of toxic DNA damage during late prophase I of yeast meiosis.Chromosoma · 2019Article
- Article
- The RecQ helicase Sgs1 drives ATP-dependent disruption of Rad51 filaments.Nucleic acids research · 2019Article
- Helicase Mechanisms During Homologous Recombination inAnnual review of biophysics · 2019Review
- Biochemical attributes of mitotic and meiotic presynaptic complexes.DNA repair · 2018Review
- Meiosis-specific recombinase Dmc1 is a potent inhibitor of the Srs2 antirecombinase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Single-Stranded DNA Curtains for Studying the Srs2 Helicase Using Total Internal Reflection Fluorescence Microscopy.Methods in enzymology · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homologous recombination is associated with the dynamic assembly and disassembly of DNA-protein complexes. Assembly of a nucleoprotein filament comprising ssDNA and the RecA homolog, Rad51, is a key step required for homology search during recombination. The budding yeast Srs2 DNA translocase is known to dismantle Rad51 filament in vitro. However, there is limited evidence to support the dismantling activity of Srs2 in vivo. Here, we show that Srs2 indeed disrupts Rad51-containing complexes from chromosomes during meiosis. Overexpression of Srs2 during the meiotic prophase impairs meiotic recombination and removes Rad51 from meiotic chromosomes. This dismantling activity is specific for Rad51, as Srs2 Overexpression does not remove Dmc1 (a meiosis-specific Rad51 homolog), Rad52 (a Rad51 mediator), or replication protein A (RPA; a single-stranded DNA-binding protein). Rather, RPA replaces Rad51 under these conditions. A mutant Srs2 lacking helicase activity cannot remove Rad51 from meiotic chromosomes. Interestingly, the Rad51-binding domain of Srs2, which is critical for Rad51-dismantling activity in vitro, is not essential for this activity in vivo. Our results suggest that a precise level of Srs2, in the form of the Srs2 translocase, is required to appropriately regulate the Rad51 nucleoprotein filament dynamics during meiosis.
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