ArticleNucleic acids research2008
Srs2 removes deadly recombination intermediates independently of its interaction with SUMO-modified PCNA.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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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
30 citing papers in PubMed, 36 citations in OpenAlex.
- Roles of Srs2/PARI-family DNA helicases in NoCut checkpoint signaling and abscission regulation.The Journal of cell biology · 2025Article
- 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
- Moving forward one step back at a time: reversibility during homologous recombination.Current genetics · 2019Review
- Intricate SUMO-based control of the homologous recombination machinery.Genes & development · 2019Review
- Yeast Lacking the PP2A Phosphatase Regulatory Subunit Rts1 SensitizesFrontiers in genetics · 2019Article
- Article
- Break-induced replication promotes formation of lethal joint molecules dissolved by Srs2.Nature communications · 2017Article
- Srs2 promotes synthesis-dependent strand annealing by disrupting DNA polymerase δ-extending D-loops.eLife · 2017Article
- Differential requirement of Srs2 helicase and Rad51 displacement activities in replication of hairpin-forming CAG/CTG repeats.Nucleic acids research · 2017Article
- Article
- Genome maintenance in Saccharomyces cerevisiae: the role of SUMO and SUMO-targeted ubiquitin ligases.Nucleic acids research · 2017Review
- Multifunctional roles of Saccharomyces cerevisiae Srs2 protein in replication, recombination and repair.FEMS yeast research · 2017Review
- SUMOylation of Rad52-Rad59 synergistically change the outcome of mitotic recombination.DNA repair · 2016Article
- Pro-recombination Role of Srs2 Protein Requires SUMO (Small Ubiquitin-like Modifier) but Is Independent of PCNA (Proliferating Cell Nuclear Antigen) Interaction.The Journal of biological chemistry · 2016Article
- Novel function of the Fanconi anemia group J or RECQ1 helicase to disrupt protein-DNA complexes in a replication protein A-stimulated manner.The Journal of biological chemistry · 2014Article
- Readers of PCNA modifications.Chromosoma · 2013Review
- Srs2 mediates PCNA-SUMO-dependent inhibition of DNA repair synthesis.The EMBO journal · 2013Article
- Srs2 prevents Rad51 filament formation by repetitive motion on DNA.Nature communications · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saccharomyces cerevisiae Srs2 helicase plays at least two distinct functions. One is to prevent recombinational repair through its recruitment by sumoylated Proliferating Cell Nuclear Antigen (PCNA), evidenced in postreplication-repair deficient cells, and a second one is to eliminate potentially lethal intermediates formed by recombination proteins. Both actions are believed to involve the capacity of Srs2 to displace Rad51 upon translocation on single-stranded DNA (ssDNA), though a role of its helicase activity may be important to remove some toxic recombination structures. Here, we described two new mutants, srs2R1 and srs2R3, that have lost the ability to hinder recombinational repair in postreplication-repair mutants, but are still able to remove toxic recombination structures. Although the mutants present very similar phenotypes, the mutated proteins are differently affected in their biochemical activities. Srs2R1 has lost its capacity to interact with sumoylated PCNA while the biochemical activities of Srs2R3 are attenuated (ATPase, helicase, DNA binding and ability to displace Rad51 from ssDNA). In addition, crossover (CO) frequencies are increased in both mutants. The different roles of Srs2, in relation to its eventual recruitment by sumoylated PCNA, are discussed.
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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.