Evidence map›Paper›PMID 20371517›Full record

ArticleNucleic acids research2010

Rad52 SUMOylation affects the efficiency of the DNA repair.

Veronika Altmannova, Nadine Eckert-Boulet, Milica Arneric, Peter Kolesar, Radka Chaloupkova, Jiri Damborsky, Patrick Sung, Xiaolan Zhao, Michael Lisby, Lumir Krejci

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

67 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Targeting RAD52 overcomes PARP inhibitor resistance in preclinicalbioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Histone modification inComputational and structural biotechnology journal · 2023
    Review
  10. Review
  11. Article
  12. Histone sumoylation and chromatin dynamics.Nucleic acids research · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Cancers · 2019
    Review
  19. Review
  20. Review

7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Veronika AltmannovaDepartment of Biology, Masaryk University, Brno, Czech Republic.
Nadine Eckert-Boulet
Milica Arneric
Peter Kolesar
Radka Chaloupkova
Jiri Damborsky
Patrick Sung
Xiaolan Zhao
Michael Lisby
Lumir Krejci
Memorial Sloan Kettering Cancer Center · USMasaryk University · CZ

Funding

YEAST DNA REPAIR GENES AND PROTEINS OF THE RAD52 GROUPR01ES007061 · NIEHS · YALE UNIVERSITY · PI Patrick Sung · 1995 to 2026
$9.4M
The Rtt107 interactome structures and functionsR01GM080670 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI ZHAO, XIAOLAN · 2007 to 2021
$4.5M
NIEHS NIH HHS R01ES07061NIGMS NIH HHS R01 GM080670NIGMS NIH HHS R01GM080670Wellcome Trust WT076476
6 · The paper itself

Abstract

Homologous recombination (HR) plays a vital role in DNA metabolic processes including meiosis, DNA repair, DNA replication and rDNA homeostasis. HR defects can lead to pathological outcomes, including genetic diseases and cancer. Recent studies suggest that the post-translational modification by the small ubiquitin-like modifier (SUMO) protein plays an important role in mitotic and meiotic recombination. However, the precise role of SUMOylation during recombination is still unclear. Here, we characterize the effect of SUMOylation on the biochemical properties of the Saccharomyces cerevisiae recombination mediator protein Rad52. Interestingly, Rad52 SUMOylation is enhanced by single-stranded DNA, and we show that SUMOylation of Rad52 also inhibits its DNA binding and annealing activities. The biochemical effects of SUMO modification in vitro are accompanied by a shorter duration of spontaneous Rad52 foci in vivo and a shift in spontaneous mitotic recombination from single-strand annealing to gene conversion events in the SUMO-deficient Rad52 mutants. Taken together, our results highlight the importance of Rad52 SUMOylation as part of a 'quality control' mechanism regulating the efficiency of recombination and DNA repair.

Indexed as

DNA RepairRecombination, GeneticDNA, Single-StrandedLysineProtein Structure, TertiaryRad51 RecombinaseRad52 DNA Repair and Recombination ProteinReplication Protein ASaccharomyces cerevisiae ProteinsSUMO-1 ProteinDNA, Single-StrandedLysineRAD51 protein, S cerevisiaeRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRAD52 protein, S cerevisiaeReplication Protein ASaccharomyces cerevisiae ProteinsSUMO-1 Protein

Identifiers

PMID20371517
PMCPMC2919706
OpenAlexW1963798045

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.