Evidence map›Paper›PMID 34255843›Full record

ArticleNucleic acids research2021

Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA.

Dukas Jurėnas, Amaury Payelleville, Mohammad Roghanian, Kathryn J Turnbull, Alain Givaudan, Julien Brillard, Vasili Hauryliuk, Eric Cascales

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

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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

8 authors at 4 institutions in 3 countries.

Dukas JurėnasLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université - CNRS, UMR 7255, Marseille, France.
Amaury PayellevilleLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université - CNRS, UMR 7255, Marseille, France.
Mohammad RoghanianDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden.
Kathryn J TurnbullDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden.
Alain GivaudanDGIMI, Univ Montpellier, INRAE, Montpellier, France.
Julien BrillardDGIMI, Univ Montpellier, INRAE, Montpellier, France.ORCID 0000-0001-9089-4834
Vasili HauryliukDepartment of Molecular Biology, Umeå University, 901 87 Umeå, Sweden.ORCID 0000-0003-2389-5057
Eric CascalesLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université - CNRS, UMR 7255, Marseille, France.ORCID 0000-0003-0611-9179
Centre National de la Recherche Scientifique · FRUmeå University · SEUniversité de Montpellier · FRLund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria have evolved sophisticated mechanisms to deliver potent toxins into bacterial competitors or into eukaryotic cells in order to destroy rivals and gain access to a specific niche or to hijack essential metabolic or signaling pathways in the host. Delivered effectors carry various activities such as nucleases, phospholipases, peptidoglycan hydrolases, enzymes that deplete the pools of NADH or ATP, compromise the cell division machinery, or the host cell cytoskeleton. Effectors categorized in the family of polymorphic toxins have a modular structure, in which the toxin domain is fused to additional elements acting as cargo to adapt the effector to a specific secretion machinery. Here we show that Photorhabdus laumondii, an entomopathogen species, delivers a polymorphic antibacterial toxin via a type VI secretion system. This toxin inhibits protein synthesis in a NAD+-dependent manner. Using a biotinylated derivative of NAD, we demonstrate that translation is inhibited through ADP-ribosylation of the ribosomal 23S RNA. Mapping of the modification further showed that the adduct locates on helix 44 of the thiostrepton loop located in the GTPase-associated center and decreases the GTPase activity of the EF-G elongation factor.

Indexed as

ADP-RibosylationBacterial ToxinsGTP PhosphohydrolasesNADPeptide Elongation Factor GPhotorhabdusProtein BiosynthesisRNA, Ribosomal, 23SThiostreptonType VI Secretion SystemsBacterial ToxinsGTP PhosphohydrolasesNADPeptide Elongation Factor GRNA, Ribosomal, 23SThiostreptonType VI Secretion Systems

Identifiers

PMID34255843
PMCPMC8661411
OpenAlexW3183090963

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.