Evidence map›Paper›PMID 22333533›Full record

ArticleGenes & development2012

Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI).

Elie J Diner, Christina M Beck, Julia S Webb, David A Low, Christopher S Hayes

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing 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

72 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
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  8. Pathogenicity assessment of Shiga toxin-producingFrontiers in microbiology · 2023
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. A phage mechanism for selective nicking of dUMP-containing DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Contact-Dependent Growth Inhibition in Bacteria: Do Not Get Too Close!International journal of molecular sciences · 2020
    Review
  17. Review
  18. Review
  19. Article
  20. Review

12 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

5 authors at 1 institution in 1 country.

Elie J DinerDepartment of Molecular, Cellular, and Developmental Biology, University of California at Santa Barbara, CA 93106, USA.
Christina M Beck
Julia S Webb
David A Low
Christopher S Hayes
University of California, Santa Barbara · US

Funding

Vaccines and Diagnostics TrialsU54AI065359 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI BARBOUR, ALAN G. · 2005 to 2013
$88.8M
Molecular determinants of A-site mRNA cleavage ribosomeR01GM078634 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI HAYES, CHRISTOPHER S. · 2006 to 2014
$2.5M
NIAID NIH HHS U54 AI065359NIAID NIH HHS U54AI065359NIGMS NIH HHS GM078634NIGMS NIH HHS R01 GM078634
6 · The paper itself

Abstract

Bacterial contact-dependent growth inhibition (CDI) is mediated by the CdiB/CdiA family of two-partner secretion proteins. CdiA effector proteins are exported onto the surface of CDI(+) inhibitor cells, where they interact with susceptible bacteria and deliver effectors/toxins derived from their C-terminal regions (CdiA-CT). CDI(+) cells also produce an immunity protein that binds the CdiA-CT and blocks its activity to prevent autoinhibition. Here, we show that the CdiA-CT from uropathogenic Escherichia coli strain 536 (UPEC536) is a latent tRNase that requires activation by the biosynthetic enzyme CysK (O-acetylserine sulfhydrylase A). UPEC536 CdiA-CT exhibits no nuclease activity in vitro, but cleaves within transfer RNA (tRNA) anti-codon loops when purified CysK is added. CysK and CdiA-CT form a stable complex, and their binding interaction appears to mimic that of the CysK/CysE cysteine synthase complex. CdiA-CT activation is also required for growth inhibition. Synthesis of CdiA-CT in E. coli cysK(+) cells arrests cell growth, whereas the growth of ΔcysK mutants is unaffected by the toxin. Moreover, E. coli ΔcysK cells are completely resistant to inhibitor cells expressing UPEC536 CdiA, indicating that CysK is required to activate the tRNase during CDI. Thus, CysK acts as a permissive factor for CDI, providing a potential mechanism to modulate growth inhibition in target cells.

Indexed as

Amino Acid SequenceCoenzymesContact InhibitionCysteine SynthaseEnzyme ActivationEscherichia coliEscherichia coli ProteinsMembrane ProteinsMolecular Sequence DataProtein BindingSequence AlignmentCdiA protein, E coliCoenzymesCysteine SynthaseEscherichia coli ProteinsMembrane Proteins

Identifiers

PMID22333533
PMCPMC3305988
OpenAlexW2143300357

What OpenQuestion holds

Textmetadata
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.