Evidence map›Paper›PMID 31028385›Full record

ArticleNucleic acids research2019

Single-molecule live cell imaging of Rep reveals the dynamic interplay between an accessory replicative helicase and the replisome.

Aisha H Syeda, Adam J M Wollman, Alex L Hargreaves, Jamieson A L Howard, Jan-Gert Brüning, Peter McGlynn, Mark C Leake

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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 64 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

7 authors at 1 institution in 1 country.

Aisha H SyedaDepartment of Physics, University of York, York YO10 5DD, UK.
Adam J M WollmanDepartment of Physics, University of York, York YO10 5DD, UK.
Alex L HargreavesDepartment of Physics, University of York, York YO10 5DD, UK.
Jamieson A L HowardDepartment of Physics, University of York, York YO10 5DD, UK.
Jan-Gert BrüningDepartment of Biology, University of York, York YO10 5DD, UK.
Peter McGlynnDepartment of Biology, University of York, York YO10 5DD, UK.
Mark C LeakeDepartment of Physics, University of York, York YO10 5DD, UK.
University of York · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N006453/1Wellcome Trust 204829
6 · The paper itself

Abstract

DNA replication must cope with nucleoprotein barriers that impair efficient replisome translocation. Biochemical and genetic studies indicate accessory helicases play essential roles in replication in the presence of nucleoprotein barriers, but how they operate inside the cell is unclear. With high-speed single-molecule microscopy we observed genomically-encoded fluorescent constructs of the accessory helicase Rep and core replisome protein DnaQ in live Escherichia coli cells. We demonstrate that Rep colocalizes with 70% of replication forks, with a hexameric stoichiometry, indicating maximal occupancy of the single DnaB hexamer. Rep associates dynamically with the replisome with an average dwell time of 6.5 ms dependent on ATP hydrolysis, indicating rapid binding then translocation away from the fork. We also imaged PriC replication restart factor and observe Rep-replisome association is also dependent on PriC. Our findings suggest two Rep-replisome populations in vivo: one continually associating with DnaB then translocating away to aid nucleoprotein barrier removal ahead of the fork, another assisting PriC-dependent reloading of DnaB if replisome progression fails. These findings reveal how a single helicase at the replisome provides two independent ways of underpinning replication of protein-bound DNA, a problem all organisms face as they replicate their genomes.

Indexed as

DNA ReplicationAdenosine TriphosphateDNA-Directed DNA PolymeraseDNA HelicasesDNA Polymerase IIIEscherichia coli ProteinsMultienzyme ComplexesProtein Interaction Domains and MotifsReplisomesSingle Molecule ImagingAdenosine TriphosphateDNA-Directed DNA PolymeraseDNA HelicasesDNA Polymerase IIIdnaQ protein, E coliEscherichia coli ProteinsMultienzyme ComplexesPriC protein, E coliReplisomesrep protein, E coli

Identifiers

PMID31028385
PMCPMC6614839
OpenAlexW2953035795

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.