Evidence map›Paper›PMID 29985128›Full record

ArticleeLife2018

Rad52-Rad51 association is essential to protect Rad51 filaments against Srs2, but facultative for filament formation.

Emilie Ma, Pauline Dupaigne, Laurent Maloisel, Raphaël Guerois, Eric Le Cam, Eric Coïc

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

25 citing papers in PubMed, 33 citations in OpenAlex.

  1. Mechanisms That Govern Recombinase Fidelity Control During Eukaryotic Homologous Recombination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Rtt105 stimulates Rad51-ssDNA assembly and orchestrates Rad51 and RPA actions to promote homologous recombination repair.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Rad54 and Rdh54 prevent Srs2-mediated disruption of Rad51 presynaptic filaments.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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

6 authors at 2 institutions in 1 country.

Emilie MaDRF, IBFJ, iRCM, CEA, Fontenay-aux-Roses, France.
Pauline DupaigneUniversité Paris-Saclay, Paris, France.
Laurent MaloiselDRF, IBFJ, iRCM, CEA, Fontenay-aux-Roses, France.
Raphaël GueroisUniversité Paris-Saclay, Paris, France.
Eric Le CamUniversité Paris-Saclay, Paris, France.
Eric CoïcDRF, IBFJ, iRCM, CEA, Fontenay-aux-Roses, France.ORCID http://orcid.org/0000-0002-9549-8969
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homology search and strand exchange mediated by Rad51 nucleoprotein filaments are key steps of the homologous recombination process. In budding yeast, Rad52 is the main mediator of Rad51 filament formation, thereby playing an essential role. The current model assumes that Rad51 filament formation requires the interaction between Rad52 and Rad51. However, we report here that Rad52 mutations that disrupt this interaction do not affect γ-ray- or HO endonuclease-induced gene conversion frequencies. In vivo and in vitro studies confirmed that Rad51 filaments formation is not affected by these mutations. Instead, we found that Rad52-Rad51 association makes Rad51 filaments toxic in Srs2-deficient cells after exposure to DNA damaging agents, independently of Rad52 role in Rad51 filament assembly. Importantly, we also demonstrated that Rad52 is essential for protecting Rad51 filaments against dissociation by the Srs2 DNA translocase. Our findings open new perspectives in the understanding of the role of Rad52 in eukaryotes.

Indexed as

AllelesAmino Acid SequenceDNA Breaks, Double-StrandedDNA, FungalDNA HelicasesGene ConversionHomologous RecombinationModels, BiologicalMutant ProteinsMutationProtein BindingProtein DomainsRad51 RecombinaseRad52 DNA Repair and Recombination ProteinSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA, FungalDNA HelicasesMutant ProteinsRAD51 protein, S cerevisiaeRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRAD52 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSRS2 protein, S cerevisiaebiochemistrychemical biologychromosomesgene expressiongenome stabilityhomologous recombinationRad51Rad52Saccharomyces cerevisiaeS. cerevisiaeSrs2

Identifiers

PMID29985128
PMCPMC6056232
OpenAlexW2854373346

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.