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

Dukas Jurėnas (), Leonardo Talachia Rosa, Martial Rey, Julia Chamot-Rooke, Rémi Fronzes () and Eric Cascales ()
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Dukas Jurėnas: Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université – CNRS, UMR 7255
Leonardo Talachia Rosa: Structure and Function of Bacterial Nanomachines, Institut Européen de Chimie et Biologie, Univ. Bordeaux – CNRS, UMR 5234 Microbiologie Fondamentale et Pathogénicité
Martial Rey: Mass Spectrometry for Biology Unit, Department of Structural Biology and Chemistry, Institut Pasteur – CNRS, USR 2000
Julia Chamot-Rooke: Mass Spectrometry for Biology Unit, Department of Structural Biology and Chemistry, Institut Pasteur – CNRS, USR 2000
Rémi Fronzes: Structure and Function of Bacterial Nanomachines, Institut Européen de Chimie et Biologie, Univ. Bordeaux – CNRS, UMR 5234 Microbiologie Fondamentale et Pathogénicité
Eric Cascales: Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université – CNRS, UMR 7255

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: Abstract 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.

Date: 2021
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DOI: 10.1038/s41467-021-27388-0

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