Evidence map›Paper›PMID 27484483›Full record

ArticleNucleic acids research2016

An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.

Tricia A Windgassen, James L Keck

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  7. Review
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  11. Dynamics of the PriA Helicase at Stalled DNA Replication Forks.The journal of physical chemistry. B · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Review
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

2 authors at 1 institution in 1 country.

Tricia A WindgassenDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USA.
James L KeckDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USA jlkeck@wisc.edu.
University of Wisconsin–Madison · 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

Helicases couple ATP hydrolysis to nucleic acid binding and unwinding via molecular mechanisms that remain poorly defined for most enzyme subfamilies within the superfamily 2 (SF2) helicase group. A crystal structure of the PriA SF2 DNA helicase, which governs restart of prematurely terminated replication processes in bacteria, revealed the presence of an aromatic-rich loop (ARL) on the presumptive DNA-binding surface of the enzyme. The position and sequence of the ARL was similar to loops known to couple ATP hydrolysis with DNA binding in a subset of other SF2 enzymes, however, the roles of the ARL in PriA had not been investigated. Here, we show that changes within the ARL sequence uncouple PriA ATPase activity from DNA binding. In vitro protein-DNA crosslinking experiments define a residue- and nucleotide-specific interaction map for PriA, showing that the ARL binds replication fork junctions whereas other sites bind the leading or lagging strands. We propose that DNA binding to the ARL allosterically triggers ATP hydrolysis in PriA. Additional SF2 helicases with similarly positioned loops may also couple DNA binding to ATP hydrolysis using related mechanisms.

Indexed as

Protein Interaction Domains and MotifsAdenosine TriphosphateAmino Acid SubstitutionCarrier ProteinsDNADNA HelicasesDNA ReplicationEnzyme ActivationEscherichia coli ProteinsHydrolysisModels, MolecularMolecular ConformationMutationProtein BindingReplication OriginStructure-Activity RelationshipAdenosine TriphosphateCarrier ProteinsDNADNA HelicasesEscherichia coli ProteinspriA protein, E coli

Identifiers

PMID27484483
PMCPMC5175346
OpenAlexW2506234310

What OpenQuestion holds

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LicenceCC BY-NC
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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.