Evidence map›Paper›PMID 23562643›Full record

ArticleCell2013

The bacterial DnaC helicase loader is a DnaB ring breaker.

Ernesto Arias-Palomo, Valerie L O'Shea, Iris V Hood, James M Berger

Abstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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  5. Article
  6. Article
  7. The Archaeal Cell Cycle.Annual review of cell and developmental biology · 2024
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. International journal of molecular sciences · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021
    Review

5 more citing papers are in PubMed but not listed here.

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.

Ernesto Arias-PalomoDepartment of Molecular and Cell Biology, California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA.
Valerie L O'Shea
Iris V Hood
James M Berger

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
MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
Investigation of DnaB helicase loading for initiating DNA replicationF32GM090803 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI O'SHEA, VALERIE LYNN · 2010 to 2011
$104k
NIGMS NIH HHS F32 GM090803NIGMS NIH HHS F32GM090803NIGMS NIH HHS R01 GM071747NIGMS NIH HHS R01-GM071747NIGMS NIH HHS R01 GM105404NIGMS NIH HHS T32 GM007232
6 · The paper itself

Abstract

Dedicated AAA+ ATPases deposit hexameric ring-shaped helicases onto DNA to promote replication in cellular organisms. To understand how loading occurs, we used electron microscopy and small angle X-ray scattering (SAXS) to determine the ATP-bound structure of the intact E. coli DnaB⋅DnaC helicase/loader complex. The 480 kDa dodecamer forms a three-tiered assembly, in which DnaC adopts a spiral configuration that remodels N-terminal scaffolding and C-terminal motor regions of DnaB to produce a clear break in the helicase ring. Surprisingly, DnaC's AAA+ fold is dispensable for ring remodeling because the DnaC isolated helicase-binding domain can both load DnaB onto DNA and increase the efficiency by which the helicase acts on substrates in vitro. Our data demonstrate that DnaC opens DnaB by a mechanism akin to that of polymerase clamp loaders and indicate that bacterial replicative helicases, like their eukaryotic counterparts, possess autoregulatory elements that influence how hexameric motor domains are loaded onto and unwind DNA.

Indexed as

DnaB HelicasesDNA ReplicationEscherichia coliEscherichia coli ProteinsGeobacillus stearothermophilusMicroscopy, ElectronModels, MolecularProtein Structure, TertiaryScattering, Small AngleDnaB HelicasesdnaB protein, E coliDnaC protein, E coliEscherichia coli Proteins

Identifiers

PMID23562643
PMCPMC3670212

What OpenQuestion holds

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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.