Evidence map›Paper›PMID 20081207›Full record

ArticleNucleic acids research2010

Human Rad52 binds and wraps single-stranded DNA and mediates annealing via two hRad52-ssDNA complexes.

Jill M Grimme, Masayoshi Honda, Rebecca Wright, Yusuke Okuno, Eli Rothenberg, Alexander V Mazin, Taekjip Ha, Maria Spies

Open 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. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

105 citing papers in PubMed, 142 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Monomers and short oligomers of human RAD52 promote single-strand annealing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. RAD52 prevents accumulation ofbioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Twinkle-Catalyzed Toehold-Mediated DNA Strand Displacement Reaction.Journal of the American Chemical Society · 2023
    Article
  20. Article

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

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 4 institutions in 1 country.

Jill M GrimmeDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Masayoshi Honda
Rebecca Wright
Yusuke Okuno
Eli Rothenberg
Alexander V Mazin
Taekjip Ha
Maria Spies
University of Illinois Urbana-Champaign · USHoward Hughes Medical Institute · USDrexel University · USU.S. Army Engineer Research and Development Center · US

Funding

Single Molecule Study of Helicase MechanismsR01GM065367 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HA, TAEKJIP · 2002 to 2014
$3.6M
Repair of DNA breaks in human: the role of Rad54 proteinR01CA100839 · NCI · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2003 to 2013
$2.6M
Repair of DNA breaks in humans: the role of Rad54 proteinR56CA100839 · NCI · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2008 to 2008
$260k
A Screen for Modulators of Human Rad51, a Key DNA Repair ProteinR03MH084119 · NIMH · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2008 to 2008
$25k
Howard Hughes Medical InstituteNCI NIH HHS CA100839NIGMS NIH HHS GM065367NIGMS NIH HHS R01 GM065367NIMH NIH HHS MH084119
6 · The paper itself

Abstract

Rad52 promotes the annealing of complementary strands of DNA bound by replication protein A (RPA) during discrete repair pathways. Here, we used a fluorescence resonance energy transfer (FRET) between two fluorescent dyes incorporated into DNA substrates to probe the mechanism by which human Rad52 (hRad52) interacts with and mediates annealing of ssDNA-hRPA complexes. Human Rad52 bound ssDNA or ssDNA-hRPA complex in two, concentration-dependent modes. At low hRad52 concentrations, ssDNA was wrapped around the circumference of the protein ring, while at higher protein concentrations, ssDNA was stretched between multiple hRad52 rings. Annealing by hRad52 occurred most efficiently when each complementary DNA strand or each ssDNA-hRPA complex was bound by hRad52 in a wrapped configuration, suggesting homology search and annealing occur via two hRad52-ssDNA complexes. In contrast to the wild type protein, hRad52(RQK/AAA) and hRad52(1-212) mutants with impaired ability to bind hRPA protein competed with hRPA for binding to ssDNA and failed to counteract hRPA-mediated duplex destabilization highlighting the importance of hRad52-hRPA interactions in promoting efficient DNA annealing.

Indexed as

Binding, CompetitiveDNA, Single-StrandedFluorescence Resonance Energy TransferHumansMutationProtein BindingRad52 DNA Repair and Recombination ProteinReplication Protein ADNA, Single-StrandedRad52 DNA Repair and Recombination ProteinRAD52 protein, humanReplication Protein A

Identifiers

PMID20081207
PMCPMC2875008
OpenAlexW2010143311

What OpenQuestion holds

Textmetadata
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.