Cargando…
Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA
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...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8661411/ https://www.ncbi.nlm.nih.gov/pubmed/34255843 http://dx.doi.org/10.1093/nar/gkab608 |
_version_ | 1784613361920507904 |
---|---|
author | Jurėnas, Dukas Payelleville, Amaury Roghanian, Mohammad Turnbull, Kathryn J Givaudan, Alain Brillard, Julien Hauryliuk, Vasili Cascales, Eric |
author_facet | Jurėnas, Dukas Payelleville, Amaury Roghanian, Mohammad Turnbull, Kathryn J Givaudan, Alain Brillard, Julien Hauryliuk, Vasili Cascales, Eric |
author_sort | Jurėnas, Dukas |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8661411 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-86614112021-12-10 Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA Jurėnas, Dukas Payelleville, Amaury Roghanian, Mohammad Turnbull, Kathryn J Givaudan, Alain Brillard, Julien Hauryliuk, Vasili Cascales, Eric Nucleic Acids Res RNA and RNA-protein complexes 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. Oxford University Press 2021-07-13 /pmc/articles/PMC8661411/ /pubmed/34255843 http://dx.doi.org/10.1093/nar/gkab608 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | RNA and RNA-protein complexes Jurėnas, Dukas Payelleville, Amaury Roghanian, Mohammad Turnbull, Kathryn J Givaudan, Alain Brillard, Julien Hauryliuk, Vasili Cascales, Eric Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA |
title |
Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA |
title_full |
Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA |
title_fullStr |
Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA |
title_full_unstemmed |
Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA |
title_short |
Photorhabdus antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of 23S ribosomal RNA |
title_sort | photorhabdus antibacterial rhs polymorphic toxin inhibits translation through adp-ribosylation of 23s ribosomal rna |
topic | RNA and RNA-protein complexes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8661411/ https://www.ncbi.nlm.nih.gov/pubmed/34255843 http://dx.doi.org/10.1093/nar/gkab608 |
work_keys_str_mv | AT jurenasdukas photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna AT payellevilleamaury photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna AT roghanianmohammad photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna AT turnbullkathrynj photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna AT givaudanalain photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna AT brillardjulien photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna AT hauryliukvasili photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna AT cascaleseric photorhabdusantibacterialrhspolymorphictoxininhibitstranslationthroughadpribosylationof23sribosomalrna |