Evidence map›Paper›PMID 30869136›Full record

ArticleNucleic acids research2019

Direct removal of RNA polymerase barriers to replication by accessory replicative helicases.

Michelle Hawkins, Juachi U Dimude, Jamieson A L Howard, Abigail J Smith, Mark S Dillingham, Nigel J Savery, Christian J Rudolph, Peter McGlynn

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. A superfamily 1 helicase translocates on double-stranded DNA.bioRxiv : the preprint server for biology · 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

8 authors at 3 institutions in 1 country.

Michelle HawkinsDepartment of Biology, University of York, Wentworth Way, York YO10 5DD, UK.
Juachi U DimudeDivision of Biosciences, College of Health and Life Sciences, Brunel University London, Uxbridge UB8 3PH, UK.
Jamieson A L HowardDepartment of Biology, University of York, Wentworth Way, York YO10 5DD, UK.
Abigail J SmithDNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Mark S DillinghamDNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Nigel J SaveryDNA-Protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Christian J RudolphDivision of Biosciences, College of Health and Life Sciences, Brunel University London, Uxbridge UB8 3PH, UK.
Peter McGlynnDepartment of Biology, University of York, Wentworth Way, York YO10 5DD, UK.
University of Bristol · GBUniversity of York · GBBrunel University of London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I001859/2Biotechnology and Biological Sciences Research Council BB/I003142/1Biotechnology and Biological Sciences Research Council BB/K015729/1Biotechnology and Biological Sciences Research Council BB/N014863/1Biotechnology and Biological Sciences Research Council BB/N014995/1
6 · The paper itself

Abstract

Bacterial genome duplication and transcription require simultaneous access to the same DNA template. Conflicts between the replisome and transcription machinery can lead to interruption of DNA replication and loss of genome stability. Pausing, stalling and backtracking of transcribing RNA polymerases add to this problem and present barriers to replisomes. Accessory helicases promote fork movement through nucleoprotein barriers and exist in viruses, bacteria and eukaryotes. Here, we show that stalled Escherichia coli transcription elongation complexes block reconstituted replisomes. This physiologically relevant block can be alleviated by the accessory helicase Rep or UvrD, resulting in the formation of full-length replication products. Accessory helicase action during replication-transcription collisions therefore promotes continued replication without leaving gaps in the DNA. In contrast, DinG does not promote replisome movement through stalled transcription complexes in vitro. However, our data demonstrate that DinG operates indirectly in vivo to reduce conflicts between replication and transcription. These results suggest that Rep and UvrD helicases operate on DNA at the replication fork whereas DinG helicase acts via a different mechanism.

Indexed as

DNA, BacterialDNA-Directed RNA PolymerasesDNA HelicasesDNA RepairDNA ReplicationEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGenome, BacterialHigh-Throughput Nucleotide SequencingMultienzyme ComplexesTranscription, GeneticdinG protein, E coliDNA, BacterialDNA-Directed RNA PolymerasesDNA HelicasesEscherichia coli ProteinsMultienzyme Complexesrep protein, E coliUvrD protein, E coli

Identifiers

PMID30869136
PMCPMC6547429
OpenAlexW2921745634

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.