Evidence map›Paper›PMID 27244442›Full record

ArticleeLife2016

Viral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replication.

Iris V Hood, James M Berger

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Frequent nonhomologous replacement of replicative helicase loaders by viruses inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  5. Article
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  7. Review
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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

2 authors at 2 institutions in 1 country.

Iris V HoodDepartment of Molecular and Cell Biology, California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, United States.
James M BergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, United States.ORCID 0000-0002-7404-8272
Johns Hopkins University · USQB3 · US

Funding

THE MOLECULAR BASIS OF CELL FUNCTIONT32GM007232 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BILDER, DAVID, UNAL, ELCIN · 1985 to 2022
$36.4M
Structure/Function Studies of DNA Replication InitiationR01GM071747 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 2005 to 2016
$4.0M
NIGMS NIH HHS R01 GM071747NIGMS NIH HHS T32 GM007232
6 · The paper itself

Abstract

Replisome assembly requires the loading of replicative hexameric helicases onto origins by AAA+ ATPases. How loader activity is appropriately controlled remains unclear. Here, we use structural and biochemical analyses to establish how an antimicrobial phage protein interferes with the function of the Staphylococcus aureus replicative helicase loader, DnaI. The viral protein binds to the loader's AAA+ ATPase domain, allowing binding of the host replicative helicase but impeding loader self-assembly and ATPase activity. Close inspection of the complex highlights an unexpected locus for the binding of an interdomain linker element in DnaI/DnaC-family proteins. We find that the inhibitor protein is genetically coupled to a phage-encoded homolog of the bacterial helicase loader, which we show binds to the host helicase but not to the inhibitor itself. These findings establish a new approach by which viruses can hijack host replication processes and explain how loader activity is internally regulated to prevent aberrant auto-association.

Indexed as

Virus ReplicationAmino Acid MotifsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacterial ProteinsBinding SitesCloning, MolecularCrystallography, X-RayDNA HelicasesEscherichia coliGene ExpressionModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacterial ProteinsDNA HelicasesRecombinant ProteinsViral ProteinsAAA+ ATPasebacteriophagebiochemistrybiophysicshelicasehelicase loaderreplicationS. aureusstructural biologyvirus

Identifiers

PMID27244442
PMCPMC4887207
OpenAlexW2395081052

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.