Evidence map›Paper›PMID 36484105›Full record

ArticleNucleic acids research2022

Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop.

Dukas Jurėnas, Martial Rey, Deborah Byrne, Julia Chamot-Rooke, Laurent Terradot, Eric Cascales

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  6. Transition-state analysis of the arginine-specific human ADP-ribosyltransferase 1.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026
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  10. Tldi1 deficiency mediates Tlde1 self-toxic effect to regulate the adaptability ofFrontiers in cellular and infection microbiology · 2026
    Article
  11. The SPI-20 and SPI-21 T6SS gene clusters fromFrontiers in microbiology · 2026
    Article
  12. Review
  13. Article
  14. Article
  15. Deciphering theJournal of bacteriology · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Genomic analysis ofFrontiers in microbiology · 2024
    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 at 2 institutions in 1 country.

Dukas JurėnasLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université, CNRS, UMR 7255, 13009 Marseille, France.
Martial ReyMass Spectrometry for Biology Unit, Université Paris Cité, Institut Pasteur, CNRS, UAR 2024, 75015 Paris, France.
Deborah ByrneProtein Expression Facility, Institut de Microbiologie de la Méditerranée (IMM), Aix-Marseille Université, CNRS, 13009 Marseille, France.
Julia Chamot-RookeMass Spectrometry for Biology Unit, Université Paris Cité, Institut Pasteur, CNRS, UAR 2024, 75015 Paris, France.ORCID 0000-0002-9427-543X
Laurent TerradotLaboratory of Molecular Microbiology and Structural Biochemistry, Institut de Biologie et Chimie des Protéines, Centre National de la Recherche Scientifique, Université de Lyon, UMR 5086, 69367 Lyon, France.
Eric CascalesLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université, CNRS, UMR 7255, 13009 Marseille, France.ORCID 0000-0003-0611-9179
Centre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rearrangement hot spot (Rhs) proteins are members of the broad family of polymorphic toxins. Polymorphic toxins are modular proteins composed of an N-terminal region that specifies their mode of secretion into the medium or into the target cell, a central delivery module, and a C-terminal domain that has toxic activity. Here, we structurally and functionally characterize the C-terminal toxic domain of the antibacterial Rhsmain protein, TreTu, which is delivered by the type VI secretion system of Salmonella enterica Typhimurium. We show that this domain adopts an ADP-ribosyltransferase fold and inhibits protein synthesis by transferring an ADP-ribose group from NAD+ to the elongation factor Tu (EF-Tu). This modification is specifically placed on the side chain of the conserved D21 residue located on the P-loop of the EF-Tu G-domain. Finally, we demonstrate that the TriTu immunity protein neutralizes TreTu activity by acting like a lid that closes the catalytic site and traps the NAD+.

Indexed as

AAA DomainPeptide Elongation Factor TuADP Ribose TransferasesADP-RibosylationNADProtein FoldingSalmonellaADP Ribose TransferasesNADPeptide Elongation Factor Tu

Identifiers

PMID36484105
PMCPMC9825190
OpenAlexW4310947226

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.