Evidence map›Paper›PMID 25765656›Full record

ArticleNucleic acids research2015

Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates.

Melita Chavdarova, Victoria Marini, Alexandra Sisakova, Hana Sedlackova, Dana Vigasova, Steven J Brill, Michael Lisby, Lumir Krejci

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. 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 · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Melita ChavdarovaDepartment of Biology, Masaryk University, Kamenice 5/A7, Brno 625 00, Czech Republic National Centre for Biomolecular Research, Masaryk University, Kamenice 5/A4, Brno 625 00, Czech Republic.
Victoria MariniDepartment of Biology, Masaryk University, Kamenice 5/A7, Brno 625 00, Czech Republic.
Alexandra SisakovaDepartment of Biology, Masaryk University, Kamenice 5/A7, Brno 625 00, Czech Republic International Clinical Research Center, Center for Biomolecular and Cellular Engineering, St. Anne's University Hospital Brno, Brno, Czech Republic.
Hana SedlackovaDepartment of Biology, Masaryk University, Kamenice 5/A7, Brno 625 00, Czech Republic.
Dana VigasovaDepartment of Biology, Masaryk University, Kamenice 5/A7, Brno 625 00, Czech Republic Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.
Steven J BrillDepartment of Genetics, Cancer Research Institute, Vlarska 7, 833 91 Bratislava, Slovakia.
Michael LisbyDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ, USA.
Lumir KrejciDepartment of Biology, Masaryk University, Kamenice 5/A7, Brno 625 00, Czech Republic National Centre for Biomolecular Research, Masaryk University, Kamenice 5/A4, Brno 625 00, Czech Republic International Clinical Research Center, Center for Biomolecular and Cellular Engineering, St. Anne's University Hospital Brno, Brno, Czech Republic lkrejci@chemi.muni.cz.
Masaryk University · CZCancer Research Institute of the Slovak Academy of Sciences · SKRutgers, The State University of New Jersey · US

Funding

Mechanism of the BLM/Sgs1 Helicase ComplexR01GM101613 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI BRILL, STEVEN J. · 2012 to 2015
$1.3M
NIGMS NIH HHS R01 GM101613NIGMS NIH HHS R01GM101613
6 · The paper itself

Abstract

A variety of DNA lesions, secondary DNA structures or topological stress within the DNA template may lead to stalling of the replication fork. Recovery of such forks is essential for the maintenance of genomic stability. The structure-specific endonuclease Mus81-Mms4 has been implicated in processing DNA intermediates that arise from collapsed forks and homologous recombination. According to previous genetic studies, the Srs2 helicase may play a role in the repair of double-strand breaks and ssDNA gaps together with Mus81-Mms4. In this study, we show that the Srs2 and Mus81-Mms4 proteins physically interact in vitro and in vivo and we map the interaction domains within the Srs2 and Mus81 proteins. Further, we show that Srs2 plays a dual role in the stimulation of the Mus81-Mms4 nuclease activity on a variety of DNA substrates. First, Srs2 directly stimulates Mus81-Mms4 nuclease activity independent of its helicase activity. Second, Srs2 removes Rad51 from DNA to allow access of Mus81-Mms4 to cleave DNA. Concomitantly, Mus81-Mms4 inhibits the helicase activity of Srs2. Taken together, our data point to a coordinated role of Mus81-Mms4 and Srs2 in processing of recombination as well as replication intermediates.

Indexed as

Recombination, GeneticBase SequenceDNA-Binding ProteinsDNA HelicasesDNA PrimersEndonucleasesFlap EndonucleasesMicroscopy, FluorescencePolymerase Chain ReactionSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesDNA-Binding ProteinsDNA HelicasesDNA PrimersEndonucleasesFlap EndonucleasesMMS4 protein, S cerevisiaeMUS81 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSRS2 protein, S cerevisiae

Identifiers

PMID25765656
PMCPMC4402524
OpenAlexW2087033941

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.