Evidence map›Paper›PMID 33421363›Full record

ArticleMolecular cell2021

Single-molecule analysis reveals cooperative stimulation of Rad51 filament nucleation and growth by mediator proteins.

Ondrej Belan, Consuelo Barroso, Artur Kaczmarczyk, Roopesh Anand, Stefania Federico, Nicola O'Reilly, Matthew D Newton, Erik Maeots, Radoslav I Enchev, Enrique Martinez-Perez and 2 more

Open access · hybridAbstract 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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 76 citations in OpenAlex.

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  13. 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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  15. Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.bioRxiv : the preprint server for biology · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 1 country.

Ondrej BelanDSB Repair Metabolism Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Consuelo BarrosoMeiosis group, MRC-London Institute of Medical Sciences, London W12 0NN, UK.
Artur KaczmarczykDepartment of Infectious Disease, Faculty of Medicine, Imperial College London, London W12 0NN, UK; Single Molecule Imaging Group, MRC-London Institute of Medical Sciences, London W12 0NN, UK.
Roopesh AnandDSB Repair Metabolism Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Stefania FedericoPeptide Chemistry STP, The Francis Crick Institute, London NW1 1AT, UK.
Nicola O'ReillyPeptide Chemistry STP, The Francis Crick Institute, London NW1 1AT, UK.
Matthew D NewtonDepartment of Infectious Disease, Faculty of Medicine, Imperial College London, London W12 0NN, UK; Single Molecule Imaging Group, MRC-London Institute of Medical Sciences, London W12 0NN, UK.
Erik MaeotsVisual Biochemistry Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Radoslav I EnchevVisual Biochemistry Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Enrique Martinez-PerezMeiosis group, MRC-London Institute of Medical Sciences, London W12 0NN, UK.
David S RuedaDepartment of Infectious Disease, Faculty of Medicine, Imperial College London, London W12 0NN, UK; Single Molecule Imaging Group, MRC-London Institute of Medical Sciences, London W12 0NN, UK. Electronic address: david.rueda@imperial.ac.uk.
Simon J BoultonDSB Repair Metabolism Laboratory, The Francis Crick Institute, London NW1 1AT, UK. Electronic address: simon.boulton@crick.ac.uk.
The Francis Crick Institute · GBMRC London Institute of Medical Sciences · GB

Funding

Cancer Research UK FC0010048Medical Research Council FC0010048Medical Research Council M-A652-5PY60Medical Research Council MC-A658-5TY10Medical Research Council MC_U120097113Medical Research Council MC_UP_1102/5Wellcome Trust 206292/Z/17/ZWellcome Trust FC0010048Wellcome Trust P67153
6 · The paper itself

Abstract

Homologous recombination (HR) is an essential DNA double-strand break (DSB) repair mechanism, which is frequently inactivated in cancer. During HR, RAD51 forms nucleoprotein filaments on RPA-coated, resected DNA and catalyzes strand invasion into homologous duplex DNA. How RAD51 displaces RPA and assembles into long HR-proficient filaments remains uncertain. Here, we employed single-molecule imaging to investigate the mechanism of nematode RAD-51 filament growth in the presence of BRC-2 (BRCA2) and RAD-51 paralogs, RFS-1/RIP-1. BRC-2 nucleates RAD-51 on RPA-coated DNA, whereas RFS-1/RIP-1 acts as a "chaperone" to promote 3' to 5' filament growth via highly dynamic engagement with 5' filament ends. Inhibiting ATPase or mutation in the RFS-1 Walker box leads to RFS-1/RIP-1 retention on RAD-51 filaments and hinders growth. The rfs-1 Walker box mutants display sensitivity to DNA damage and accumulate RAD-51 complexes non-functional for HR in vivo. Our work reveals the mechanism of RAD-51 nucleation and filament growth in the presence of recombination mediators.

Indexed as

Recombinational DNA RepairAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCarrier ProteinsDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA, HelminthGene Expression RegulationMolecular ChaperonesMutationProtein BindingRad51 RecombinaseReplication Protein ASignal TransductionSingle Molecule ImagingBRC-2 protein, C elegansCaenorhabditis elegans ProteinsCarrier ProteinsDNA-Binding ProteinsDNA, HelminthMolecular Chaperonesrad-51 protein, C elegansRad51 RecombinaseReplication Protein ARFS-1 protein, C elegansRIP-1 protein, C elegansBRCA2DNA repairhomologous recombinationRad51 nucleoprotein filamentsRad51 paralogssingle molecule approaches

Identifiers

PMID33421363
PMCPMC7941204
OpenAlexW3120569436

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.