Evidence map›Paper›PMID 24898247›Full record

ArticleThe Journal of biological chemistry2014

Mechanisms of toxin inhibition and transcriptional repression by Escherichia coli DinJ-YafQ.

Ajchareeya Ruangprasert, Tatsuya Maehigashi, Stacey J Miles, Nisha Giridharan, Julie X Liu, Christine M Dunham

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Infection and immunity · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021
    Review
  12. Article
  13. Bioinformatic Analysis of theFrontiers in microbiology · 2021
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors.

Ajchareeya RuangprasertFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Tatsuya MaehigashiFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Stacey J MilesFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Nisha GiridharanFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Julie X LiuFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Christine M DunhamFrom the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322 christine.m.dunham@emory.edu.

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
NCRR NIH HHS P41 RR015301
6 · The paper itself

Abstract

Bacteria encounter environmental stresses that regulate a gene expression program required for adaptation and survival. Here, we report the 1.8-Å crystal structure of the Escherichia coli toxin-antitoxin complex YafQ-(DinJ)2-YafQ, a key component of the stress response. The antitoxin DinJ dimer adopts a ribbon-helix-helix motif required for transcriptional autorepression, and toxin YafQ contains a microbial RNase fold whose proposed active site is concealed by DinJ binding. Contrary to previous reports, our studies indicate that equivalent levels of transcriptional repression occur by direct interaction of either YafQ-(DinJ)2-YafQ or a DinJ dimer at a single inverted repeat of its recognition sequence that overlaps with the -10 promoter region. Surprisingly, multiple YafQ-(DinJ)2-YafQ complexes binding to the operator region do not appear to amplify the extent of repression. Our results suggest an alternative model for transcriptional autorepression that may be novel to DinJ-YafQ.

Indexed as

Bacterial ToxinsEscherichia coliEscherichia coli ProteinsModels, BiologicalRepressor ProteinsCrystallography, X-RayProtein MultimerizationProtein Structure, QuaternaryTranscription, GeneticBacterial ToxinsDinJ protein, E coliEscherichia coli ProteinsRepressor ProteinsYafQ protein, E coliBacterial ToxinEnergy MetabolismRibbon-Helix-Helix FactorStress ResponseToxin-Antitoxin ComplexesTranscription RepressorX-ray Crystallography

Identifiers

PMID24898247
PMCPMC4110269

What OpenQuestion holds

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Registered trials

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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.