Evidence map›Paper›PMID 41942263›Full record

ArticleGenes & development2026

The eukaryotic homology search complex distorts donor DNA structure to probe for homology.

Mitchell V Woodhouse, Jingyi Hu, Meiling Wu, Jin Qian, James T Inman, Michelle D Wang, J Brooks Crickard

Abstract read
In one paragraph

Article in Genes & development, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 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
    Review
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Mitchell V WoodhouseDeparment of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.
Jingyi HuDeparment of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.
Meiling WuHoward Hughes Medical Institute, Cornell University, Ithaca, New York 14853, USA.
Jin QianHoward Hughes Medical Institute, Cornell University, Ithaca, New York 14853, USA.
James T InmanHoward Hughes Medical Institute, Cornell University, Ithaca, New York 14853, USA.ORCID 0000-0003-3534-0323
Michelle D Wang *Howard Hughes Medical Institute, Cornell University, Ithaca, New York 14853, USA; jbc287@cornell.edu mdw17@cornell.edu.ORCID 0000-0001-9137-3790
J Brooks Crickard *Deparment of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA; jbc287@cornell.edu mdw17@cornell.edu.

Funding

TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
Molecular Mechanisms of Human Homologous RecombinationR35GM142457 · NIGMS · CORNELL UNIVERSITY · PI John Brooks Crickard · 2021 to 2026
$2.3M
Fundamental Biological Processes Under TorsionR01GM136894 · NIGMS · CORNELL UNIVERSITY · PI WANG, MICHELLE D. · 2020 to 2023
$1.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM136894NIGMS NIH HHS R35 GM142457NIGMS NIH HHS T32 GM008267
6 · The paper itself

Abstract

Homologous recombination (HR) is a DNA double-strand break repair pathway that facilitates genetic exchange and protects damaged replication forks during DNA synthesis. As a template-based repair process, the successful repair of a double-strand break depends on locating suitable homology from a donor DNA sequence elsewhere in the genome. In eukaryotes, Rad51 catalyzes the homology search in coordination with the ATP-dependent motor protein Rad54. The mechanism by which these two proteins regulate forces on dsDNA substrates during homology search remains unknown. Here, we have utilized single-molecule magnetic tweezers and optical trapping methods to monitor remodeling of the DNA template during the homology search. We found that the activity of Rad51 and Rad54 remodels the donor DNA substrate to control the association and dissociation of Rad51-ssDNA filaments in the absence of DNA homology. The mechanism is through the generation of short, isolated, underwound DNA loops extruded by the homology search complex composed of Rad51 and Rad54. Finally, failure of Rad54 to act processively disrupts target selection in vivo. This study provides a basic understanding of how motorized homology search manipulates the donor DNA during the search for a suitable repair template.

Indexed as

DNAHomologous RecombinationRad51 RecombinaseSaccharomyces cerevisiaeDNA HelicasesDNA Repair EnzymesDNA, Single-StrandedNuclear ProteinsNucleic Acid ConformationOptical TweezersSaccharomyces cerevisiae ProteinsDNADNA HelicasesDNA Repair EnzymesDNA, Single-StrandedNuclear ProteinsRad51 RecombinaseRAD54 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsDNA strand exchangehomologous recombinationmagnetic tweezersoptical trapRad51Rad54single molecule

Identifiers

PMID41942263
PMCPMC13119058

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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.