Evidence map›Paper›PMID 30060236›Full record

ArticleNucleic acids research2018

The 2B subdomain of Rep helicase links translocation along DNA with protein displacement.

Jan-Gert Brüning, Jamieson A L Howard, Kamila K Myka, Mark S Dillingham, Peter McGlynn

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. A superfamily 1 helicase translocates on double-stranded DNA.bioRxiv : the preprint server for biology · 2026
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  12. Regulation of E. coli Rep helicase activity by PriC.Journal of molecular biology · 2021
    Article
  13. Article
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  15. Article
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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

5 authors at 2 institutions in 1 country.

Jan-Gert BrüningDepartment of Biology, University of York, York YO10 5DD, UK.
Jamieson A L HowardDepartment of Biology, University of York, York YO10 5DD, UK.
Kamila K MykaDepartment of Biology, University of York, York YO10 5DD, UK.
Mark S DillinghamDNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Peter McGlynnDepartment of Biology, University of York, York YO10 5DD, UK.
University of York · GBUniversity of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K00168X/1
6 · The paper itself

Abstract

Helicases catalyse DNA and RNA strand separation. Proteins bound to the nucleic acid must also be displaced in order to unwind DNA. This is exemplified by accessory helicases that clear protein barriers from DNA ahead of advancing replication forks. How helicases catalyse DNA unwinding is increasingly well understood but how protein displacement is achieved is unclear. Escherichia coli Rep accessory replicative helicase lacking one of its four subdomains, 2B, has been shown to be hyperactivated for DNA unwinding in vitro but we show here that RepΔ2B is, in contrast, deficient in displacing proteins from DNA. This defect correlates with an inability to promote replication of protein-bound DNA in vitro and lack of accessory helicase function in vivo. Defective protein displacement is manifested on double-stranded and single-stranded DNA. Thus binding and distortion of duplex DNA by the 2B subdomain ahead of the helicase is not the missing function responsible for this deficiency. These data demonstrate that protein displacement from DNA is not simply achieved by helicase translocation alone. They also imply that helicases may have evolved different specific features to optimise DNA unwinding and protein displacement, both of which are now recognised as key functions in all aspects of nucleic acid metabolism.

Indexed as

Bacterial ProteinsBinding SitesDeoxyribonuclease EcoRIDNADNA, BacterialDnaB HelicasesDNA-Binding ProteinsDNA HelicasesDNA Polymerase IIIDNA PrimaseDNA ReplicationDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsGene ExpressionModels, MolecularBacterial ProteinsDeoxyribonuclease EcoRIDNADnaA protein, BacteriaDNA, BacterialDnaB HelicasesDNA-Binding ProteinsdnaB protein, E coliDnaC protein, E colidnaG protein, E coliDNA HelicasesDNA Polymerase IIIDNA PrimaseDNA, Single-StrandedEscherichia coli Proteinsrep protein, E coliSSB protein, E coli

Identifiers

PMID30060236
PMCPMC6158625
OpenAlexW2883250897

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.