Evidence map›Paper›PMID 40909483›Full record

ArticlebioRxiv : the preprint server for biology2025

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 readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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, NY 14853, USA.
Jingyi HuDeparment of Molecular Biology and Genetics, Cornell University Ithaca, NY 14853, USA.
Meiling WuHoward Hughes Medical Institute, Cornell University, Ithaca, New York; Department of Physics & LASSP, Cornell University, Ithaca, New York.
Jin QianHoward Hughes Medical Institute, Cornell University, Ithaca, New York; Department of Physics & LASSP, Cornell University, Ithaca, New York.
James T InmanHoward Hughes Medical Institute, Cornell University, Ithaca, New York; Department of Physics & LASSP, Cornell University, Ithaca, New York.ORCID 0000-0003-3534-0323
Michelle D WangHoward Hughes Medical Institute, Cornell University, Ithaca, New York; Department of Physics & LASSP, Cornell University, Ithaca, New York.ORCID 0000-0001-9137-3790
J Brooks CrickardDeparment of Molecular Biology and Genetics, Cornell University Ithaca, NY 14853, USA.

Funding

Molecular Mechanisms of Human Homologous RecombinationR35GM142457 · NIGMS · CORNELL UNIVERSITY · PI John Brooks Crickard · 2021 to 2026
$2.3M
NIGMS NIH HHS R35 GM142457
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 find 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. This mechanism occurs through the application of both linear (tension) and rotational (torsion) forces on the donor DNA. Finally, failure of Rad54 to act processively disrupts target selection

Indexed as

Homologous RecombinationMagnetic TweezersOptical TrapRad51Rad54Single moleculeStrand Exchange

Identifiers

PMID40909483
PMCPMC12407866

What OpenQuestion holds

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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.