Evidence map›Paper›PMID 32449930›Full record

ArticleNucleic acids research2020

E. coli Rep helicase and RecA recombinase unwind G4 DNA and are important for resistance to G4-stabilizing ligands.

Tapas Paul, Andrew F Voter, Rachel R Cueny, Momčilo Gavrilov, Taekjip Ha, James L Keck, Sua Myong

Abstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. A superfamily 1 helicase translocates on double-stranded DNA.bioRxiv : the preprint server for biology · 2026
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  17. G-quadruplex DNA: a novel target for drug design.Cellular and molecular life sciences : CMLS · 2021
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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.

Tapas PaulDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
Andrew F VoterDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USA.
Rachel R CuenyDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USA.
Momčilo GavrilovDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
Taekjip HaDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
James L KeckDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USA.
Sua MyongDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.

Funding

Creation and Repair of Postreplicative DNA GapsRM1GM130450 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Michael M. Cox, MYRON GOODMAN · 2019 to 2026
$10.4M
INTEGRATED TRAINING FOR PHYSICIAN-SCIENTISTST32GM008692 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BURKARD, MARK E · 1998 to 2020
$10.3M
Structure and Function of the Bacterial PrimosomeR01GM098885 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI James L Keck · 2012 to 2026
$4.0M
Quantitative Analysis of G-Quadruplex Folding and its Role in Gene ExpressionR01GM115631 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MYONG, SUA · 2016 to 2019
$1.2M
Acquisition of GE Typhoon FLA9500 Variable Mode ImagerS10OD021567 · OD · JOHNS HOPKINS UNIVERSITY · PI MCCAFFERY, J. MICHAEL · 2017 to 2017
$147k
Identification of chemosensitizing agents that block DNA repair by the Fanconi Anemia/Bloom Dissolvasome complexF30CA210465 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI VOTER, ANDREW FORD · 2016 to 2019
$118k
Howard Hughes Medical InstituteNCI NIH HHS F30 CA210465NIGMS NIH HHS R01 GM098885NIGMS NIH HHS R01 GM115631NIGMS NIH HHS RM1 GM130450NIGMS NIH HHS T32 GM008692NIH HHS S10 OD021567
6 · The paper itself

Abstract

G-quadruplex (G4) DNA structures can form physical barriers within the genome that must be unwound to ensure cellular genomic integrity. Here, we report unanticipated roles for the Escherichia coli Rep helicase and RecA recombinase in tolerating toxicity induced by G4-stabilizing ligands in vivo. We demonstrate that Rep and Rep-X (an enhanced version of Rep) display G4 unwinding activities in vitro that are significantly higher than the closely related UvrD helicase. G4 unwinding mediated by Rep involves repetitive cycles of G4 unfolding and refolding fueled by ATP hydrolysis. Rep-X and Rep also dislodge G4-stabilizing ligands, in agreement with our in vivo G4-ligand sensitivity result. We further demonstrate that RecA filaments disrupt G4 structures and remove G4 ligands in vitro, consistent with its role in countering cellular toxicity of G4-stabilizing ligands. Together, our study reveals novel genome caretaking functions for Rep and RecA in resolving deleterious G4 structures.

Indexed as

G-QuadruplexesAdenosine TriphosphateDNA-Binding ProteinsDNA HelicasesDNA ReplicationEscherichia coliEscherichia coli ProteinsLigandsNucleic Acid ConformationRec A RecombinasesAdenosine TriphosphateDNA-Binding ProteinsDNA HelicasesEscherichia coli ProteinsLigandsrecA protein, E coliRec A Recombinasesrep protein, E coliUvrD protein, E coli

Identifiers

PMID32449930
PMCPMC7337899

What OpenQuestion holds

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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.