Evidence map›Paper›PMID 21857994›Full record

ArticlePloS one2011

Subunit interface residues F129 and H294 of human RAD51 are essential for recombinase function.

Ravindra Amunugama, Richard Fishel

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 47% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Article
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

2 authors at 2 institutions in 1 country.

Ravindra AmunugamaBiophysics Graduate Program, The Ohio State University Medical Center, Columbus, Ohio, United States of America.
Richard Fishel
The Ohio State University · USThe Ohio State University Wexner Medical Center · US

Funding

Recombination/Repair Complex in Human CellsR01GM080176 · NIGMS · OHIO STATE UNIVERSITY · PI FISHEL, RICHARD · 2006 to 2015
$3.2M
NIGMS NIH HHS GM080176NIGMS NIH HHS R01 GM080176
6 · The paper itself

Abstract

RAD51 mediated homologous recombinational repair (HRR) of DNA double-strand breaks (DSBs) is essential to maintain genomic integrity. RAD51 forms a nucleoprotein filament (NPF) that catalyzes the fundamental homologous pairing and strand exchange reaction (recombinase) required for HRR. Based on structural and functional homology with archaeal and yeast RAD51, we have identified the human RAD51 (HsRAD51) subunit interface residues HsRad51(F129) in the Walker A box and HsRad51(H294) in the L2 ssDNA binding region as potentially important participants in salt-induced conformational transitions essential for recombinase activity. We demonstrate that the HsRad51(F129V) and HsRad51(H294V) substitution mutations reduce DNA dependent ATPase activity and are largely defective in the formation of a functional NPF, which ultimately eliminates recombinase catalytic functions. Our data are consistent with the conclusion that the HsRAD51(F129) and HsRAD51(H294) residues are important participants in the cation-induced allosteric activation of HsRAD51.

Indexed as

Recombinational DNA RepairAdenosine TriphosphateAmino Acid SequenceAmino Acid SubstitutionBinding SitesCatalytic DomainDNADNA Breaks, Double-StrandedDNA, Single-StrandedHistidineHumansModels, MolecularMolecular Sequence DataMutationPhenylalanineProtein SubunitsAdenosine TriphosphateDNADNA, Single-StrandedHistidinePhenylalanineProtein SubunitsRAD51 protein, humanRad51 Recombinase

Identifiers

PMID21857994
PMCPMC3155514
OpenAlexW2036803161

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.