JURĖNAS, Dukas; ROSA, Leonardo Talachia; REY, Martial; CHAMOT-ROOKE, Julia; FRONZES, Rémi; CASCALES, Eric

doi:10.1038/s41467-021-27388-0

ROSA, Leonardo Talachia
Microbiologie Fondamentale et Pathogénicité [MFP]

REY, Martial

Langue

Article de revue

Ce document a été publié dans

Nature Communications. 2021-12-01, vol. 12, n° 1, p. 6998

Résumé en anglais

Bacteria have evolved toxins to outcompete other bacteria or to hijack host cell pathways. One broad family of bacterial polymorphic toxins gathers multidomain proteins with a modular organization, comprising a C-terminal toxin domain fused to a N-terminal domain that adapts to the delivery apparatus. Polymorphic toxins include bacteriocins, contact-dependent growth inhibition systems, and specialized Hcp, VgrG, PAAR or Rhs Type VI secretion (T6SS) components. We recently described and characterized Tre23, a toxin domain fused to a T6SS-associated Rhs protein in Photorhabdus laumondii, Rhs1. Here, we show that Rhs1 forms a complex with the T6SS spike protein VgrG and the EagR chaperone. Using truncation derivatives and cross-linking mass spectrometry, we demonstrate that VgrG-EagR-Rhs1 complex formation requires the VgrG C-terminal β-helix and the Rhs1 N-terminal region. We then report the cryo-electron-microscopy structure of the Rhs1-EagR complex, demonstrating that the Rhs1 central region forms a β-barrel cage-like structure that encapsulates the C-terminal toxin domain, and provide evidence for processing of the Rhs1 protein through aspartyl autoproteolysis. We propose a model for Rhs1 loading on the T6SS, transport and delivery into the target cell.< Réduire

Mots clés en anglais

Adaptation

Physiological

Bacterial Proteins

Bacterial Toxins

Bacteriocins

Contact Inhibition

Cryoelectron Microscopy

Mass Spectrometry

Models

Molecular

Photorhabdus

Type VI Secretion Systems

URI

https://oskar-bordeaux.fr/handle/20.500.12278/202280

DOI

http://dx.doi.org/10.1038/s41467-021-27388-0

Unités de recherche

MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234

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Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin.

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Résumé en anglais

Mots clés en anglais

URI

DOI

Unités de recherche