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Architecture and assembly of the Type VI secretion system.
Zoued, Abdelrahim; Brunet, Yannick R; Durand, Eric; Aschtgen, Marie-Stéphanie; Logger, Laureen; Douzi, Badreddine; Journet, Laure; Cambillau, Christian; Cascales, Eric.
Afiliação
  • Zoued A; Laboratoire d'Ingeniérie des Systèmes Macromoléculaires, CNRS, Aix-Marseille Université, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
  • Brunet YR; Laboratoire d'Ingeniérie des Systèmes Macromoléculaires, CNRS, Aix-Marseille Université, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
  • Durand E; Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
  • Aschtgen MS; Laboratoire d'Ingeniérie des Systèmes Macromoléculaires, CNRS, Aix-Marseille Université, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
  • Logger L; Laboratoire d'Ingeniérie des Systèmes Macromoléculaires, CNRS, Aix-Marseille Université, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
  • Douzi B; Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
  • Journet L; Laboratoire d'Ingeniérie des Systèmes Macromoléculaires, CNRS, Aix-Marseille Université, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
  • Cambillau C; Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
  • Cascales E; Laboratoire d'Ingeniérie des Systèmes Macromoléculaires, CNRS, Aix-Marseille Université, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. Electronic address: cascales@imm.cnrs.fr.
Biochim Biophys Acta ; 1843(8): 1664-73, 2014 Aug.
Article em En | MEDLINE | ID: mdl-24681160
ABSTRACT
The Type VI secretion system (T6SS) delivers protein effectors to diverse cell types including prokaryotic and eukaryotic cells, therefore it participates in inter-bacterial competition and pathogenesis. The T6SS is constituted of an envelope-spanning complex anchoring a cytoplasmic tubular edifice. This tubular structure is evolutionarily, functionally and structurally related to the tail of contractile phages. It is composed of an inner tube tipped by a spike complex, and engulfed within a sheath-like structure. This structure assembles onto a platform called "baseplate" that is connected to the membrane sub-complex. The T6SS functions as a nano-crossbow upon contraction of the sheath, the inner tube is propelled towards the target cell, allowing effector delivery. This review focuses on the architecture and biogenesis of this fascinating secretion machine, highlighting recent advances regarding the assembly of the membrane or tail complexes. This article is part of a Special Issue entitled Protein trafficking and secretion in bacteria. Guest Editors Anastassios Economou and Ross Dalbey.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Transporte Proteico / Sistemas de Secreção Bacterianos Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Transporte Proteico / Sistemas de Secreção Bacterianos Idioma: En Ano de publicação: 2014 Tipo de documento: Article