Evidence map›Paper›PMID 24239291›Full record

ArticleMolecular cell2013

A bacterial toxin inhibits DNA replication elongation through a direct interaction with the β sliding clamp.

Christopher D Aakre, Tuyen N Phung, David Huang, Michael T Laub

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed, 1 pooled it
8.1field-weighted citation impact, top 2% 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

135 citing papers in PubMed, 1 synthesis or guideline pooled it, 215 citations in OpenAlex.

  1. Pooled it
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  5. Review
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  7. Article
  8. Article
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  11. Article
  12. Article
  13. Article
  14. Article
  15. Evidence for a Functional HipBA Toxin-Antitoxin System inInternational journal of molecular sciences · 2025
    Article
  16. Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025
    Review
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Christopher D AakreDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Tuyen N PhungDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
David HuangDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Michael T LaubDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: laub@mit.edu.
Howard Hughes Medical Institute · USMassachusetts Institute of Technology · US

Funding

Cell Cycle Regulation in Caulobacter CrescentusR01GM082899 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LAUB, MICHAEL · 2008 to 2020
$3.8M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM082899NIGMS NIH HHS R01GM082899
6 · The paper itself

Abstract

Toxin-antitoxin (TA) systems are ubiquitous on bacterial chromosomes, yet the mechanisms regulating their activity and the molecular targets of toxins remain incompletely defined. Here, we identify SocAB, an atypical TA system in Caulobacter crescentus. Unlike canonical TA systems, the toxin SocB is unstable and constitutively degraded by the protease ClpXP; this degradation requires the antitoxin, SocA, as a proteolytic adaptor. We find that the toxin, SocB, blocks replication elongation through an interaction with the sliding clamp, driving replication fork collapse. Mutations that suppress SocB toxicity map to either the hydrophobic cleft on the clamp that binds DNA polymerase III or a clamp-binding motif in SocB. Our findings suggest that SocB disrupts replication by outcompeting other clamp-binding proteins. Collectively, our results expand the diversity of mechanisms employed by TA systems to regulate toxin activity and inhibit bacterial growth, and they suggest that inhibiting clamp function may be a generalizable antibacterial strategy.

Indexed as

AntitoxinsBacterial ProteinsBacterial ToxinsCaulobacter crescentusChromosomes, BacterialDNA-Binding ProteinsDNA ReplicationMutationProtein BindingProteolysisAntitoxinsBacterial ProteinsBacterial ToxinsDNA-Binding Proteins

Identifiers

PMID24239291
PMCPMC3918436
OpenAlexW2170305714

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.