Evidence map›Paper›PMID 23460207›Full record

ArticleNucleic acids research2013

The Shu complex interacts with Rad51 through the Rad51 paralogues Rad55-Rad57 to mediate error-free recombination.

Stephen Godin, Adam Wier, Faiz Kabbinavar, Dominique S Bratton-Palmer, Harshad Ghodke, Bennett Van Houten, Andrew P VanDemark, Kara A Bernstein

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

43 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mechanism of mitotic recombination: insights from C. elegans.Current opinion in genetics & development · 2021
    Review
  10. RAD51 paralog function in replicative DNA damage and tolerance.Current opinion in genetics & development · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Annual review of genetics · 2020
    Review
  18. Article
  19. Review
  20. Article
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 2 institutions in 1 country.

Stephen GodinDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, University of Pittsburgh Cancer Institute, Pittsburgh, PA 15213, USA.
Adam Wier
Faiz Kabbinavar
Dominique S Bratton-Palmer
Harshad Ghodke
Bennett Van Houten
Andrew P VanDemark
Kara A Bernstein
University of Pittsburgh · USUPMC Hillman Cancer Center · US

Funding

DNA damage recognition by nucleotide excision repair proteinsR01ES019566 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI VAN HOUTEN, BENNETT · 2011 to 2020
$3.9M
Mechanistic insights into the SHU complex and Sgs1 in DNA repair and replicationR00GM088413 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BERNSTEIN, KARA A · 2011 to 2013
$772k
Mechanistic insights into the SHU complex and Sgs1 in DNA repair and replicationK99GM088413 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI BERNSTEIN, KARA A · 2009 to 2010
$180k
NIEHS NIH HHS ES019566NIEHS NIH HHS R01 ES019566NIGMS NIH HHS GM088413
6 · The paper itself

Abstract

The Saccharomyces cerevisiae Shu complex, consisting of Shu1, Shu2, Csm2 and Psy3, promotes error-free homologous recombination (HR) by an unknown mechanism. Recent structural analysis of two Shu proteins, Csm2 and Psy3, has revealed that these proteins are Rad51 paralogues and mediate DNA binding of this complex. We show in vitro that the Csm2-Psy3 heterodimer preferentially binds synthetic forked DNA or 3'-DNA overhang substrates resembling structures used during HR in vivo. We find that Csm2 interacts with Rad51 and the Rad51 paralogues, the Rad55-Rad57 heterodimer and that the Shu complex functions in the same epistasis group as Rad55-Rad57. Importantly, Csm2's interaction with Rad51 is dependent on Rad55, whereas Csm2's interaction with Rad55 occurs independently of Rad51. Consistent with the Shu complex containing Rad51 paralogues, the methyl methanesulphonate sensitivity of Csm2 is exacerbated at colder temperatures. Furthermore, Csm2 and Psy3 are needed for efficient recruitment of Rad55 to DNA repair foci after DNA damage. Finally, we observe that the Shu complex preferentially promotes Rad51-dependent homologous recombination over Rad51-independent repair. Our data suggest a model in which Csm2-Psy3 recruit the Shu complex to HR substrates, where it interacts with Rad51 through Rad55-Rad57 to stimulate Rad51 filament assembly and stability, promoting error-free repair.

Indexed as

Recombinational DNA RepairAdenosine TriphosphatasesCold TemperatureDNADNA-Binding ProteinsDNA Repair EnzymesEpistasis, GeneticMethyl MethanesulfonateRad51 RecombinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCsm2 protein, S cerevisiaeDNADNA-Binding ProteinsDNA Repair EnzymesMethyl MethanesulfonatePSY3 protein, S cerevisiaeRAD51 protein, S cerevisiaeRad51 RecombinaseRAD55 protein, S cerevisiaeRAD57 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID23460207
PMCPMC3632125
OpenAlexW1966089056

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.