Evidence map›Paper›PMID 27264868›Full record

ArticleMolecular cell2016

A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA.

Angela M Cheverton, Bridget Gollan, Michal Przydacz, Chi T Wong, Anastasia Mylona, Stephen A Hare, Sophie Helaine

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed
16.9field-weighted citation impact, top 1% 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

151 citing papers in PubMed, 234 citations in OpenAlex.

  1. Identification of genes promoting fitness of a plant-associatedApplied and environmental microbiology · 2026
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  12. Mechanisms and Pathological Significance of Liquid-Liquid Phase Separation in Bacteria.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  13. Antibiotic-recalcitrant Salmonella during infection.Nature reviews. Microbiology · 2025
    Review
  14. Article
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  16. Evidence for a Functional HipBA Toxin-Antitoxin System inInternational journal of molecular sciences · 2025
    Article
  17. Putting bacteria in alarm.Nature chemical biology · 2025
    Article
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  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Angela M ChevertonSection of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Bridget GollanSection of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Michal PrzydaczDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Chi T WongDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Anastasia MylonaSection of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Stephen A HareDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK.
Sophie HelaineSection of Microbiology, Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK. Electronic address: s.helaine@imperial.ac.uk.
Imperial College London · GBMedical Research Council · GB

Funding

Medical Research Council G1100332Medical Research Council MR/J006874/1Medical Research Council MR/M009629/1
6 · The paper itself

Abstract

The recalcitrance of many bacterial infections to antibiotic treatment is thought to be due to the presence of persisters that are non-growing, antibiotic-insensitive cells. Eventually, persisters resume growth, accounting for relapses of infection. Salmonella is an important pathogen that causes disease through its ability to survive inside macrophages. After macrophage phagocytosis, a significant proportion of the Salmonella population forms non-growing persisters through the action of toxin-antitoxin modules. Here we reveal that one such toxin, TacT, is an acetyltransferase that blocks the primary amine group of amino acids on charged tRNA molecules, thereby inhibiting translation and promoting persister formation. Furthermore, we report the crystal structure of TacT and note unique structural features, including two positively charged surface patches that are essential for toxicity. Finally, we identify a detoxifying mechanism in Salmonella wherein peptidyl-tRNA hydrolase counteracts TacT-dependent growth arrest, explaining how bacterial persisters can resume growth.

Indexed as

Drug Resistance, BacterialTransfer RNA AminoacylationAcetyltransferasesBacterial ProteinsBacterial ToxinsCarboxylic Ester HydrolasesModels, MolecularProtein ConformationRNA, BacterialRNA, TransferSalmonella typhimuriumStructure-Activity RelationshipSurface PropertiesTime FactorsVirulenceAcetyltransferasesaminoacyl-tRNA hydrolaseBacterial ProteinsBacterial ToxinsCarboxylic Ester HydrolasesRimL protein, Salmonella typhimuriumRNA, BacterialRNA, Transfer

Identifiers

PMID27264868
PMCPMC4942678
OpenAlexW2417855243

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.