Evidence map›Paper›PMID 30797687›Full record

ArticleMolecular cell2019

Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA.

Ernesto Arias-Palomo, Neha Puri, Valerie L O'Shea Murray, Qianyun Yan, James M Berger

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 72 citations in OpenAlex.

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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 2 countries.

Ernesto Arias-PalomoDepartment of Structural & Chemical Biology, Centro de Investigaciones Biológicas, CIB-CSIC 28040 Madrid, Spain. Electronic address: earias@cib.csic.es.
Neha PuriDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Valerie L O'Shea MurrayDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Qianyun YanDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
James M BergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: jmberger@jhmi.edu.
Johns Hopkins Medicine · USCentro de Investigaciones Biológicas Margarita Salas · ES

Funding

Mechanistic Studies of Replication Initiation in ProkaryotesR37GM071747 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI James M. Berger · 2017 to 2026
$4.4M
FEI Tecnai F20 Transmission Electron Microscope for Core Microscopy FacilityS10OD012342 · OD · JOHNS HOPKINS UNIVERSITY · PI MCCAFFERY, J. MICHAEL · 2014 to 2014
$1.3M
NIGMS NIH HHS R37 GM071747NIH HHS S10 OD012342Wellcome Trust
6 · The paper itself

Abstract

In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases onto DNA to initiate chromosomal replication. To better understand the mechanisms by which helicase loading can occur, we used cryo-EM to determine sub-4-Å-resolution structures of the E. coli DnaB⋅DnaC helicase⋅loader complex with nucleotide in pre- and post-DNA engagement states. In the absence of DNA, six DnaC protomers latch onto and crack open a DnaB hexamer using an extended N-terminal domain, stabilizing this conformation through nucleotide-dependent ATPase interactions. Upon binding DNA, DnaC hydrolyzes ATP, allowing DnaB to isomerize into a topologically closed, pre-translocation state competent to bind primase. Our data show how DnaC opens the DnaB ring and represses the helicase prior to DNA binding and how DnaC ATPase activity is reciprocally regulated by DnaB and DNA. Comparative analyses reveal how the helicase loading mechanism of DnaC parallels and diverges from homologous AAA+ systems involved in DNA replication and transposition.

Indexed as

DNA ReplicationAdenosine TriphosphateBinding SitesCryoelectron MicroscopyDNA, BacterialDnaB HelicasesDNA PrimaseEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialHydrolysisModels, MolecularNucleic Acid ConformationProtein BindingProtein ConformationStructure-Activity RelationshipAdenosine TriphosphateDNA, BacterialDnaB HelicasesdnaB protein, E coliDnaC protein, E coliDNA PrimaseEscherichia coli Proteins

Identifiers

PMID30797687
PMCPMC6450724
OpenAlexW2916162831

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.