The mechanism of force transmission at bacterial focal adhesion complexes

Laura M. Faure, Jean-Bernard Fiche, Leon Espinosa, Adrien Ducret, Vivek Anantharaman, Jennifer Luciano, Sébastien Lhospice, Salim T. Islam, Julie Tréguier, Mélanie Sotes, Erkin Kuru, Michael S. Van Nieuwenhze, Yves V. Brun, Olivier Théodoly, L. Aravind, Marcelo Nollmann () and Tâm Mignot ()
Additional contact information
Laura M. Faure: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Jean-Bernard Fiche: Centre de Biochimie Structurale, CNRS UMR5048, INSERM U1054, Montpellier University
Leon Espinosa: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Adrien Ducret: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Vivek Anantharaman: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
Jennifer Luciano: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Sébastien Lhospice: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Salim T. Islam: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Julie Tréguier: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Mélanie Sotes: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée
Erkin Kuru: Interdisciplinary Biochemistry Program, Indiana University
Michael S. Van Nieuwenhze: Indiana University
Yves V. Brun: Indiana University
Olivier Théodoly: Adhesion and Inflammation laboratory, INSERM U1067, Aix Marseille University
L. Aravind: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
Marcelo Nollmann: Centre de Biochimie Structurale, CNRS UMR5048, INSERM U1054, Montpellier University
Tâm Mignot: Laboratoire de Chimie Bactérienne, CNRS-Aix Marseille University UMR7283, Institut de Microbiologie de la Méditerranée

Nature, 2016, vol. 539, issue 7630, 530-535

Abstract: Abstract Various rod-shaped bacteria mysteriously glide on surfaces in the absence of appendages such as flagella or pili. In the deltaproteobacterium Myxococcus xanthus, a putative gliding motility machinery (the Agl–Glt complex) localizes to so-called focal adhesion sites (FASs) that form stationary contact points with the underlying surface. Here we show that the Agl–Glt machinery contains an inner-membrane motor complex that moves intracellularly along a right-handed helical path; when the machinery becomes stationary at FASs, the motor complex powers a left-handed rotation of the cell around its long axis. At FASs, force transmission requires cyclic interactions between the molecular motor and the adhesion proteins of the outer membrane via a periplasmic interaction platform, which presumably involves contractile activity of motor components and possible interactions with peptidoglycan. Our results provide a molecular model of bacterial gliding motility.

Date: 2016
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DOI: 10.1038/nature20121

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