Evidence map›Paper›PMID 33421364›Full record

ArticleMolecular cell2021

The Rad51 paralog complex Rad55-Rad57 acts as a molecular chaperone during homologous recombination.

Upasana Roy, Youngho Kwon, Lea Marie, Lorraine Symington, Patrick Sung, Michael Lisby, Eric C Greene

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 64 citations in OpenAlex.

  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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  14. Rtt105 stimulates Rad51-ssDNA assembly and orchestrates Rad51 and RPA actions to promote homologous recombination repair.Proceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Upasana RoyDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Youngho KwonDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
Lea MarieDepartment of Microbiology and Immunology, Columbia University, New York, NY 10032, USA.
Lorraine SymingtonDepartment of Microbiology and Immunology, Columbia University, New York, NY 10032, USA.
Patrick SungDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
Michael LisbyDepartment of Biology, University of Copenhagen, 2200 Copenhagen N, Denmark; Center for Chromosome Stability, Department of Cellular and Molecular Medicine, University of Copenhagen, 2200 Copenhagen N, Denmark.
Eric C GreeneDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. Electronic address: ecg2108@cumc.columbia.edu.
Columbia University · USThe University of Texas Health Science Center at San Antonio · USColumbia University Irving Medical Center · USUniversity of Copenhagen · DK

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
YEAST DNA REPAIR GENES AND PROTEINS OF THE RAD52 GROUPR01ES007061 · NIEHS · YALE UNIVERSITY · PI Patrick Sung · 1995 to 2026
$9.4M
Mechanisms of DNA Homology-directed Genome Repair and Tumor SuppressionR35CA241801 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI SUNG, PATRICK · 2019 to 2025
$6.0M
Mechanism and regulation of DNA double-strand break repairR35GM126997 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Lorraine S Symington · 2018 to 2026
$5.9M
Protein purification instrumentation in support of single molecule studies of genome integrityR35GM118026 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GREENE, ERIC C · 2016 to 2025
$5.7M
Helicase regulation during homologous recombinationR01CA236606 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Eric C Greene · 2019 to 2026
$2.6M
Defining the contributions of BRCA1, BRCA2, and RAD52 to genome stabilityR01CA221858 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GREENE, ERIC C · 2020 to 2024
$1.9M
NCI NIH HHS P01 CA092584NCI NIH HHS R01 CA221858NCI NIH HHS R01 CA236606NCI NIH HHS R35 CA241801NIEHS NIH HHS R01 ES007061NIGMS NIH HHS R35 GM118026NIGMS NIH HHS R35 GM126997Wellcome TrustWellcome Trust 206292/D/17/Z
6 · The paper itself

Abstract

Homologous recombination (HR) is essential for maintenance of genome integrity. Rad51 paralogs fulfill a conserved but undefined role in HR, and their mutations are associated with increased cancer risk in humans. Here, we use single-molecule imaging to reveal that the Saccharomyces cerevisiae Rad51 paralog complex Rad55-Rad57 promotes assembly of Rad51 recombinase filament through transient interactions, providing evidence that it acts like a classical molecular chaperone. Srs2 is an ATP-dependent anti-recombinase that downregulates HR by actively dismantling Rad51 filaments. Contrary to the current model, we find that Rad55-Rad57 does not physically block the movement of Srs2. Instead, Rad55-Rad57 promotes rapid re-assembly of Rad51 filaments after their disruption by Srs2. Our findings support a model in which Rad51 is in flux between free and single-stranded DNA (ssDNA)-bound states, the rate of which is controlled dynamically though the opposing actions of Rad55-Rad57 and Srs2.

Indexed as

Gene Expression Regulation, FungalHomologous RecombinationAdenosine TriphosphatasesBinding SitesDNA-Binding ProteinsDNA, FungalDNA HelicasesDNA Repair EnzymesDNA, Single-StrandedGenes, ReporterGreen Fluorescent ProteinsLuminescent ProteinsMolecular ChaperonesMutationProtein BindingRad51 RecombinaseAdenosine TriphosphatasesDNA-Binding ProteinsDNA, FungalDNA HelicasesDNA Repair EnzymesDNA, Single-StrandedGreen Fluorescent ProteinsLuminescent ProteinsMolecular ChaperonesRAD51 protein, S cerevisiaeRad51 RecombinaseRAD55 protein, S cerevisiaeRAD57 protein, S cerevisiaeRed Fluorescent ProteinSaccharomyces cerevisiae ProteinsSRS2 protein, S cerevisiaeDNA curtainsDNA repairhomologous recombinationRad51Rad51 paralogsRad55-Rad57single-moleculeSrs2

Identifiers

PMID33421364
PMCPMC8262405
OpenAlexW3118998329

What OpenQuestion holds

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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.