Evidence map›Paper›PMID 34423481›Full record

ArticleMolecular microbiology2021

Escherichia coli K-12 has two distinguishable PriA-PriB replication restart pathways.

Steven J Sandler, Maxime Leroux, Tricia A Windgassen, James L Keck

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

9 citing papers in PubMed, 10 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

4 authors at 2 institutions in 2 countries.

Steven J SandlerDepartment of Microbiology, University of Massachusetts at Amherst, Amherst, Massachusetts, USA.ORCID 0000-0003-2994-1552
Maxime LerouxDepartment of Microbiology, University of Massachusetts at Amherst, Amherst, Massachusetts, USA.
Tricia A WindgassenDepartment of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, USA.
James L KeckDepartment of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, USA.
University of Wisconsin–Madison · USMcGill University · CA

Funding

Structure and Function of the Bacterial PrimosomeR01GM098885 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI James L Keck · 2012 to 2026
$4.0M
NIGMS NIH HHS R01 GM098885
6 · The paper itself

Abstract

In Escherichia coli, PriA, PriB, PriC, and DnaT proteins mediate three pathways for Replication Restart called PriA-PriB, PriA-PriC, and PriC. PriA is crucial for two of the three pathways. Its absence leads to slow growth, high basal levels of SOS expression, poorly partitioning nucleoids, UV sensitivity, and recombination deficiency. PriA has ATPase and helicase activities and interacts with PriB, DnaT, and single-stranded DNA-binding protein (SSB). priA300 (K230R) and priA301 (C479Y) have no phenotype as single mutants, but each phenocopy a priA-null mutant combined with ∆priB. This suggested that the two priA mutations affected the helicase activity that is required for the PriA-PriC pathway. To further test this, the biochemical activities of purified PriA300 and PriA301 were examined. As expected, PriA300 lacks ATPase and helicase activities but retains the ability to interact with PriB. PriA301, however, retains significant PriB-stimulated helicase activity even though PriA301 interactions with PriB and DNA are weakened. A PriA300,301 variant retains only the ability to interact with DNA in vitro and phenocopies the priA-null phenotype in vivo. This suggests that there are two biochemically and genetically distinct PriA-PriB pathways. One uses PriB-stimulated helicase activity to free a region of ssDNA and the other uses helicase-independent remodeling activity.

Indexed as

DNA, BacterialDNA-Binding ProteinsDNA HelicasesDNA ReplicationEscherichia coli K12Escherichia coli ProteinsMutationDNA, BacterialDNA-Binding ProteinsDNA HelicasesDnaT protein, E coliEscherichia coli ProteinspriA protein, E coliPriB protein, E coliPriC protein, E coliDNA repairDNA replicationhomologous recombinationreplication restartSOS response

Identifiers

PMID34423481
PMCPMC8541903
OpenAlexW3193356045

What OpenQuestion holds

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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.