Evidence map›Paper›PMID 41326376›Full record

ArticleNature communications2025

RAD51 D-loop structures reveal the mechanism of eukaryotic RAD51-mediated strand exchange.

Shih-Chi Luo, Cheng-Han Yang, Hsin-Yi Yeh, Cheng-Wei Lin, Min-Chi Yeh, Peter Chi, Meng-Chiao Ho

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Mechanisms That Govern Recombinase Fidelity Control During Eukaryotic Homologous Recombination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
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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

7 authors.

Shih-Chi LuoInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0000-0001-7723-3230
Cheng-Han YangInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0000-0001-7517-3799
Hsin-Yi YehInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Cheng-Wei LinInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Min-Chi YehInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0009-0000-1499-7719
Peter ChiInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0000-0001-9229-8729
Meng-Chiao HoInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan. joeho@as.edu.tw.ORCID http://orcid.org/0000-0002-5424-4524

Funding

Academia Sinica AS-TP-112-L01
6 · The paper itself

Abstract

Strand exchange is a key step in homologous recombination, enabling template-based repair of DNA double-strand breaks. Eukaryotic RAD51 forms an ATP-dependent helical presynaptic filament on single-stranded DNA (ssDNA), which then searches for homologous double-stranded DNA (dsDNA), and catalyzes the strand exchange to form a D-loop in an ATP hydrolysis-independent manner. The molecular mechanism by which RAD51 facilitates dsDNA unwinding and pairing remains unclear. Here, we present cryo-EM structures of RAD51 mini-filaments bound to homologous dsDNA, capturing five intermediates from dsDNA recruitment to D-loop formation. These structures, together with molecular dynamics simulations, suggest a stepwise mechanism: the conserved N-terminal domain (NTD) recruits and bends the dsDNA, weakening base pairing near the exchange site. Subsequent engagement with positively-charged regions, including the loop L2 and loop Arg303-Arg306, further bends the homologous dsDNA, thereby not only positioning it closer to the strand exchange site but also inducing local base-pair opening. Additionally, the loop L2 (Met278 and Phe279) inserts between strands, and the secondary DNA binding sites (S2 sites) capture the displaced strand to prevent strand reannealing. Together, our findings provide detailed insight into a spatially coordinated mechanism of strand exchange by RAD51.

Indexed as

Rad51 RecombinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCryoelectron MicroscopyDNADNA Breaks, Double-StrandedDNA, Single-StrandedHomologous RecombinationMolecular Dynamics SimulationProtein BindingDNADNA, Single-StrandedRAD51 protein, S cerevisiaeRad51 RecombinaseSaccharomyces cerevisiae Proteins

Identifiers

PMID41326376
PMCPMC12783270

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.