Evidence map›Paper›PMID 23182424›Full record

ArticleDNA repair2013

Role of the conserved lysine within the Walker A motif of human DMC1.

Deepti Sharma, Amanda F Say, LeAnna L Ledford, Ami J Hughes, Hilarie A Sehorn, Donard S Dwyer, Michael G Sehorn

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Microbiology spectrum · 2026
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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

7 authors at 2 institutions in 1 country.

Deepti SharmaDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Amanda F Say
LeAnna L Ledford
Ami J Hughes
Hilarie A Sehorn
Donard S Dwyer
Michael G Sehorn
Clemson University · USLouisiana State University Health Sciences Center Shreveport · US

Funding

Role of Mei5-Sae3 in meiotic homologous recombinationR01GM098510 · NIGMS · CLEMSON UNIVERSITY · PI SEHORN, MICHAEL G. · 2011 to 2015
$1.2M
Howard Hughes Medical Institute 52005867NIGMS NIH HHS GM098510NIGMS NIH HHS R01 GM098510
6 · The paper itself

Abstract

During meiosis, the RAD51 recombinase and its meiosis-specific homolog DMC1 mediate DNA strand exchange between homologous chromosomes. The proteins form a right-handed nucleoprotein complex on ssDNA called the presynaptic filament. In an ATP-dependent manner, the presynaptic filament searches for homology to form a physical connection with the homologous chromosome. We constructed two variants of hDMC1 altering the conserved lysine residue of the Walker A motif to arginine (hDMC1(K132R)) or alanine (hDMC1(K132A)). The hDMC1 variants were expressed in Escherichia coli and purified to near homogeneity. Both hDMC1(K132R) and hDMC1(K132A) variants were devoid of ATP hydrolysis. The hDMC1(K132R) variant was attenuated for ATP binding that was partially restored by the addition of either ssDNA or calcium. The hDMC1(K132R) variant was partially capable of homologous DNA pairing and strand exchange in the presence of calcium and protecting DNA from a nuclease, while the hDMC1(K132A) variant was inactive. These results suggest that the conserved lysine of the Walker A motif in hDMC1 plays a key role in ATP binding. Furthermore, the binding of calcium and ssDNA promotes a conformational change in the ATP binding pocket of hDMC1 that promotes ATP binding. Our results provide evidence that the conserved lysine in the Walker A motif of hDMC1 is critical for ATP binding which is required for presynaptic filament formation.

Indexed as

Adenosine TriphosphateAlanineAmino Acid MotifsAmino Acid SequenceArginineBinding SitesCalciumCell Cycle ProteinsDNA-Binding ProteinsDNA, Single-StrandedHumansHydrolysisLysineMolecular Sequence DataMutation, MissenseProtein Structure, TertiaryAdenosine TriphosphateAlanineArginineCalciumCell Cycle ProteinsDMC1 protein, humanDNA-Binding ProteinsDNA, Single-StrandedLysine

Identifiers

PMID23182424
PMCPMC3677694
OpenAlexW1988625327

What OpenQuestion holds

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LicenceTDM
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.