Evidence map›Paper›PMID 33300032›Full record

ArticleNucleic acids research2021

A skipping rope translocation mechanism in a widespread family of DNA repair helicases.

Johann J Roske, Sunbin Liu, Bernhard Loll, Ursula Neu, Markus C Wahl

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. A superfamily 1 helicase translocates on double-stranded DNA.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Bacterial DNA excision repair pathways.Nature reviews. Microbiology · 2022
    Review
  10. Article
  11. Large-scale ratcheting in a bacterial DEAH/RHA-type RNA helicase that modulates antibiotics susceptibility.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

5 authors at 2 institutions in 1 country.

Johann J RoskeFreie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustraβe 6, D-14195 Berlin, Germany.
Sunbin LiuFreie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustraβe 6, D-14195 Berlin, Germany.
Bernhard LollFreie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustraβe 6, D-14195 Berlin, Germany.
Ursula NeuFreie Universität Berlin, Institute of Chemistry and Biochemistry, Biochemistry of Viruses, Takustraβe 6, D-14195 Berlin, Germany.
Markus C WahlFreie Universität Berlin, Institute of Chemistry and Biochemistry, Laboratory of Structural Biochemistry, Takustraβe 6, D-14195 Berlin, Germany.
Freie Universität Berlin · DEHelmholtz-Zentrum Berlin für Materialien und Energie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitomycin repair factor A represents a family of DNA helicases that harbor a domain of unknown function (DUF1998) and support repair of mitomycin C-induced DNA damage by presently unknown molecular mechanisms. We determined crystal structures of Bacillus subtilis Mitomycin repair factor A alone and in complex with an ATP analog and/or DNA and conducted structure-informed functional analyses. Our results reveal a unique set of auxiliary domains appended to a dual-RecA domain core. Upon DNA binding, a Zn2+-binding domain, encompassing the domain of unknown function, acts like a drum that rolls out a canopy of helicase-associated domains, entrapping the substrate and tautening an inter-domain linker across the loading strand. Quantification of DNA binding, stimulated ATPase and helicase activities in the wild type and mutant enzyme variants in conjunction with the mode of coordination of the ATP analog suggest that Mitomycin repair factor A employs similar ATPase-driven conformational changes to translocate on DNA, with the linker ratcheting through the nucleotides like a 'skipping rope'. The electrostatic surface topology outlines a likely path for the displaced DNA strand. Our results reveal unique molecular mechanisms in a widespread family of DNA repair helicases linked to bacterial antibiotics resistance.

Indexed as

DNA RepairModels, ChemicalAdenosine TriphosphateBacillus subtilisBacterial ProteinsCrystallography, X-RayDNADNA DamageDNA HelicasesDrug Resistance, MicrobialModels, MolecularMolecular Motor ProteinsMultigene FamilyNucleoside-TriphosphataseProtein BindingProtein ConformationAdenosine TriphosphateBacterial ProteinsDNADNA HelicasesMolecular Motor ProteinsNucleoside-TriphosphataseRecombinant ProteinsZinc

Identifiers

PMID33300032
PMCPMC7797055
OpenAlexW3111285977

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.