Evidence map›Paper›PMID 30201718›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.

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

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-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

31 citing papers in PubMed, 42 citations in OpenAlex.

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  17. Dynamics of the PriA Helicase at Stalled DNA Replication Forks.The journal of physical chemistry. B · 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

5 authors at 2 institutions in 1 country.

Tricia A WindgassenDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706.
Maxime LerouxDepartment of Microbiology, University of Massachusetts Amherst, Amherst, MA 01003.
Kenneth A SatyshurDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706.
Steven J SandlerDepartment of Microbiology, University of Massachusetts Amherst, Amherst, MA 01003.
James L KeckDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706; jlkeck@wisc.edu.ORCID 0000-0002-5961-0220
University of Wisconsin–Madison · USUniversity of Massachusetts Amherst · US

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

DNA replication restart, the essential process that reinitiates prematurely terminated genome replication reactions, relies on exquisitely specific recognition of abandoned DNA replication-fork structures. The PriA DNA helicase mediates this process in bacteria through mechanisms that remain poorly defined. We report the crystal structure of a PriA/replication-fork complex, which resolves leading-strand duplex DNA bound to the protein. Interaction with PriA unpairs one end of the DNA and sequesters the 3'-most nucleotide from the nascent leading strand into a conserved protein pocket. Cross-linking studies reveal a surface on the winged-helix domain of PriA that binds to parental duplex DNA. Deleting the winged-helix domain alters PriA's structure-specific DNA unwinding properties and impairs its activity in vivo. Our observations lead to a model in which coordinated parental-, leading-, and lagging-strand DNA binding provide PriA with the structural specificity needed to act on abandoned DNA replication forks.

Indexed as

DNA ReplicationModels, BiologicalCrystallography, X-RayDNA, BacterialDNA HelicasesEscherichia coliEscherichia coli ProteinsProtein DomainsProtein Structure, SecondaryStructure-Activity RelationshipDNA, BacterialDNA HelicasesEscherichia coli ProteinspriA protein, E colicross-link mappingDNA repairDNA replication restartprotein–DNA complexX-ray crystallography

Identifiers

PMID30201718
PMCPMC6166810
OpenAlexW2891905845

What OpenQuestion holds

Textmetadata
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.