Evidence map›Paper›PMID 28369041›Full record

ArticleNature chemical biology2017

AtaT blocks translation initiation by N-acetylation of the initiator tRNA

Dukas Jurėnas, Sneha Chatterjee, Albert Konijnenberg, Frank Sobott, Louis Droogmans, Abel Garcia-Pino, Laurence Van Melderen

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Putting bacteria in alarm.Nature chemical biology · 2025
    Article
  3. Article
  4. Article
  5. Influence of NMolecules (Basel, Switzerland) · 2024
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Identification of Type II Toxin-Antitoxin Loci in Levilactobacillus brevis.Interdisciplinary sciences, computational life sciences · 2022
    Article
  15. Article
  16. Review
  17. Bugs on Drugs: AMicroorganisms · 2022
    Article
  18. Article
  19. Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021
    Review
  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

7 authors at 3 institutions in 3 countries.

Dukas JurėnasLaboratoire de Génétique et Physiologie Bactérienne, Université Libre de Bruxelles, Gosselies, Belgium.
Sneha ChatterjeeBiomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, Antwerp, Belgium.
Albert KonijnenbergBiomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, Antwerp, Belgium.
Frank SobottBiomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, Antwerp, Belgium.
Louis DroogmansLaboratoire de Microbiologie, Université Libre de Bruxelles, Gosselies, Belgium.
Abel Garcia-PinoLaboratoire de Biologie Structurale et Biophysique, Université Libre de Bruxelles, Gosselies, Belgium.
Laurence Van MelderenLaboratoire de Génétique et Physiologie Bactérienne, Université Libre de Bruxelles, Gosselies, Belgium.ORCID 0000-0002-7778-1736
Université Libre de Bruxelles · BEUniversity of Antwerp · BEUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Toxin-antitoxin (TA) loci are prevalent in bacterial genomes. They are suggested to play a central role in dormancy and persister states. Under normal growth conditions, TA toxins are neutralized by their cognate antitoxins, and under stress conditions, toxins are freed and inhibit essential cellular processes using a variety of mechanisms. Here we characterize ataR-ataT, a novel TA system, from enterohemorrhagic Escherichia coli. We show that the toxin AtaT is a GNAT family enzyme that transfers an acetyl group from acetyl coenzyme A to the amine group of the methionyl aminoacyl moiety of initiator tRNA. AtaT specifically modifies Met-tRNA

Indexed as

Escherichia coliAcetylationAmino-Acid N-AcetyltransferaseElectrophoresis, Gel, Two-DimensionalGene Expression RegulationModels, BiologicalProtein BiosynthesisRNA, Transfer, MetAmino-Acid N-AcetyltransferaseRNA, Transfer, Met

Identifiers

PMID28369041
OpenAlexW2604858366

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.