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Priming and polymerization of a bacterial contractile tail structure

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  • Abdelrahim Zoued

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université)

  • Eric Durand

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université
    Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique
    Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université
    G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur)

  • Yannick R. Brunet

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université
    † Present address: Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachussets 02115, USA.)

  • Silvia Spinelli

    (Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique
    Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université)

  • Badreddine Douzi

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université
    Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique
    Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université)

  • Mathilde Guzzo

    (Laboratoire de Chimie Bactérienne, Institut de Microbiologie de la Méditerranée, CNRS UMR7283, Aix-Marseille Université)

  • Nicolas Flaugnatti

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université)

  • Pierre Legrand

    (Synchrotron Soleil, L’Orme des merisiers)

  • Laure Journet

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université)

  • Rémi Fronzes

    (G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur
    UMR 3528, CNRS, Institut Pasteur)

  • Tâm Mignot

    (Laboratoire de Chimie Bactérienne, Institut de Microbiologie de la Méditerranée, CNRS UMR7283, Aix-Marseille Université)

  • Christian Cambillau

    (Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique
    Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université)

  • Eric Cascales

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université)

Abstract

Contractile tails are composed of an inner tube wrapped by an outer sheath assembled in an extended, metastable conformation that stores mechanical energy necessary for its contraction. Contraction is used to propel the rigid inner tube towards target cells for DNA or toxin delivery. Although recent studies have revealed the structure of the contractile sheath of the type VI secretion system, the mechanisms by which its polymerization is controlled and coordinated with the assembly of the inner tube remain unknown. Here we show that the starfish-like TssA dodecameric complex interacts with tube and sheath components. Fluorescence microscopy experiments in enteroaggregative Escherichia coli reveal that TssA binds first to the type VI secretion system membrane core complex and then initiates tail polymerization. TssA remains at the tip of the growing structure and incorporates new tube and sheath blocks. On the basis of these results, we propose that TssA primes and coordinates tail tube and sheath biogenesis.

Suggested Citation

  • Abdelrahim Zoued & Eric Durand & Yannick R. Brunet & Silvia Spinelli & Badreddine Douzi & Mathilde Guzzo & Nicolas Flaugnatti & Pierre Legrand & Laure Journet & Rémi Fronzes & Tâm Mignot & Christian C, 2016. "Priming and polymerization of a bacterial contractile tail structure," Nature, Nature, vol. 531(7592), pages 59-63, March.
  • Handle: RePEc:nat:nature:v:531:y:2016:i:7592:d:10.1038_nature17182
    DOI: 10.1038/nature17182
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    Cited by:

    1. Steven J. Jensen & Bonnie J. Cuthbert & Fernando Garza-Sánchez & Colette C. Helou & Rodger Miranda & Celia W. Goulding & Christopher S. Hayes, 2024. "Advanced glycation end-product crosslinking activates a type VI secretion system phospholipase effector protein," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Selina Fecht & Patricia Paracuellos & Sujatha Subramoni & Casandra Ai Zhu Tan & Aravindan Ilangovan & Tiago R. D. Costa & Alain Filloux, 2024. "Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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