Evidence map›Paper›PMID 35351361›Full record

ReviewTrends in biochemical sciences2022

Convergent evolution in two bacterial replicative helicase loaders.

Jillian Chase, James Berger, David Jeruzalmi

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

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

3 authors at 2 institutions in 1 country.

Jillian ChaseDepartment of Chemistry and Biochemistry, City College of New York, New York, NY 10031, USA; PhD Program in Biochemistry, The Graduate Center of the City University of New York, New York, NY 10016, USA.
James BergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA. Electronic address: jmberger@jhmi.edu.
David JeruzalmiDepartment of Chemistry and Biochemistry, City College of New York, New York, NY 10031, USA; PhD Program in Biochemistry, The Graduate Center of the City University of New York, New York, NY 10016, USA; PhD Program in Biology, The Graduate Center of the City University of New York, New York, NY 10016, USA; PhD Program in Chemistry, The Graduate Center of the City University of New York, New York, NY 10016, USA. Electronic address: dj@ccny.cuny.edu.
The Graduate Center, CUNY · USBloomberg (United States) · US

Funding

Mechanistic Studies of Replication Initiation in ProkaryotesR37GM071747 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI James M. Berger · 2017 to 2026
$4.4M
Replication Initiation in Bacteria and EukaryotesR01GM084162 · NIGMS · HARVARD UNIVERSITY · PI JERUZALMI, DAVID · 2009 to 2012
$1.5M
NIGMS NIH HHS R01 GM084162NIGMS NIH HHS R37 GM071747
6 · The paper itself

Abstract

Dedicated loader proteins play essential roles in bacterial DNA replication by opening ring-shaped DnaB-family helicases and chaperoning single-stranded (ss)DNA into a central motor chamber as a prelude to DNA unwinding. Although unrelated in sequence, the Escherichia coli DnaC and bacteriophage λ P loaders feature a similar overall architecture: a globular domain linked to an extended lasso/grappling hook element, located at their N and C termini, respectively. Both loaders remodel a closed DnaB ring into nearly identical right-handed open conformations. The sole element shared by the loaders is a single alpha helix, which binds to the same site on the helicase. Physical features of the loaders establish that DnaC and λ P evolved independently to converge, through molecular mimicry, on a common helicase-opening mechanism.

Indexed as

Escherichia coli ProteinsBacterial ProteinsDnaB HelicasesDNA HelicasesDNA ReplicationDNA, Single-StrandedEscherichia coliBacterial ProteinsDnaB HelicasesDNA HelicasesDNA, Single-StrandedEscherichia coli Proteinsconvergent evolutionDnaBDnaC, λ PDNA replicationhelicase loading

Identifiers

PMID35351361
PMCPMC9189051
OpenAlexW4220776840

What OpenQuestion holds

Textmetadata
LicenceTDM
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.