Bacillus subtilis MutL samples multiple conformations during nucleotide binding and hydrolysis.

Javier Rodríguez González, Corey L Davis, Hunter Wilkins, Dorothy A Erie, Alba Guarné

Erratum issuedAbstract read

In one paragraph

Article in Structure (London, England : 1993), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Two Glu/Asp residues cooperatively mediate an early step of ATP hydrolysis in GHKL ATPases MutL and GyrB.eLife · 2026
Article

4 · The record

Corrections and comments

Erratum issued
Bacillus subtilis MutL samples multiple conformations during nucleotide binding and hydrolysis.2026

5 · Who and what money

Authors and funding

5 authors.

Javier Rodríguez GonzálezDepartment of Biochemistry and Centre de Recherche en Biologie Structurale, McGill University, Montreal, QC, Canada.

Corey L DavisDepartment of Chemistry, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, USA.

Hunter WilkinsDepartment of Chemistry, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, USA.

Dorothy A ErieDepartment of Chemistry, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, USA.

Alba GuarnéDepartment of Biochemistry and Centre de Recherche en Biologie Structurale, McGill University, Montreal, QC, Canada. Electronic address: alba.guarne@mcgill.ca.

Funding

Integrative single molecule studies: DNA repair and technology developmentR35GM127151 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOROTHY A ERIE · 2018 to 2026

$4.6M

NIGMS NIH HHS R35 GM127151

6 · The paper itself

Abstract

DNA mismatch repair is an evolutionarily conserved repair pathway that corrects replication errors, thereby preventing genome instability. Two evolutionarily conserved proteins, MutS and MutL, recognize the mismatch and mark the newly synthesized strand for repair. Previous studies have shown how bacterial MutS homodimers function asymmetrically to recognize mismatches and recruit MutL. However, whether MutL homodimers also function asymmetrically to coordinate binding to MutS and activation of their nuclease activity remains unclear. Here, we characterize the ATPase domain of Bacillus subtilis MutL, a MutL protein with endonuclease activity, and delineate the differences with Escherichia coli MutL, a homolog without endonuclease activity. We find that B. subtilis MutL has low affinity for ATP and samples a repertoire of conformations that resemble those observed in eukaryotic MutL paralogs, indicating a relationship between ATP-induced dimer compaction and nuclease activity.

Indexed as

Adenosine TriphosphateBacillus subtilisBacterial ProteinsMutL ProteinsBinding SitesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsHydrolysisModels, MolecularProtein BindingProtein ConformationProtein MultimerizationAdenosine TriphosphateBacterial ProteinsEscherichia coli ProteinsMutL protein, E coliMutL Proteinsatomic force microscopyconformational changesDNA mismatch repairGHKL ATPasesMutLprotein dynamicstransient protein interactionsX-ray crystallography

Identifiers

PMID41478286

DOI10.1016/j.str.2025.12.007

PMCPMC13054617

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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.