Evidence map›Paper›PMID 26271032›Full record

ArticlePLoS biology2015

A Single-Strand Annealing Protein Clamps DNA to Detect and Secure Homology.

Marcel Ander, Sivaraman Subramaniam, Karim Fahmy, A Francis Stewart, Erik Schäffer

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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
  5. A structural phylogenetic tree of Rad52 and its annealase superfamily.Computational and structural biotechnology journal · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Structure and mechanism of the Red recombination system of bacteriophage λ.Progress in biophysics and molecular biology · 2019
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Marcel AnderNanomechanics Group, Biotechnology Center, TU Dresden, Dresden, Germany.
Sivaraman SubramaniamDepartment of Genomics, Biotechnology Center, TU Dresden, Dresden, Germany.
Karim FahmyDivision of Biophysics, Institute of Resource Ecology, Helmholtz-Zentrum Dresden-Rossendorf, Dresden, Germany.
A Francis StewartDepartment of Genomics, Biotechnology Center, TU Dresden, Dresden, Germany.
Erik SchäfferNanomechanics Group, Biotechnology Center, TU Dresden, Dresden, Germany; Cellular Nanoscience, Center for Plant Molecular Biology (ZMBP), Universität Tübingen, Tübingen, Germany.
TU Dresden · DEHelmholtz-Zentrum Dresden-Rossendorf · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Repair of DNA breaks by single-strand annealing (SSA) is a major mechanism for the maintenance of genomic integrity. SSA is promoted by proteins (single-strand-annealing proteins [SSAPs]), such as eukaryotic RAD52 and λ phage Redβ. These proteins use a short single-stranded region to find sequence identity and initiate homologous recombination. However, it is unclear how SSAPs detect homology and catalyze annealing. Using single-molecule experiments, we provide evidence that homology is recognized by Redβ monomers that weakly hold single DNA strands together. Once annealing begins, dimerization of Redβ clamps the double-stranded region and nucleates nucleoprotein filament growth. In this manner, DNA clamping ensures and secures a successful detection for DNA sequence homology. The clamp is characterized by a structural change of Redβ and a remarkable stability against force up to 200 pN. Our findings not only present a detailed explanation for SSAP action but also identify the DNA clamp as a very stable, noncovalent, DNA-protein interaction.

Indexed as

Sequence Homology, Nucleic AcidBacteriophage lambdaBlotting, WesternDNA-Binding ProteinsDNA RepairDNA, Single-StrandedDNA, ViralElectrophoresis, Polyacrylamide GelEscherichia coliModels, BiologicalViral ProteinsDNA-Binding ProteinsDNA, Single-StrandedDNA, ViralViral Proteins

Identifiers

PMID26271032
PMCPMC4535883
OpenAlexW1562361795

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.