Journal
NATURE
Volume 539, Issue 7630, Pages 530-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/nature20121
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Funding
- Fondation ARC
- Fondation pour la Recherche Medicale
- Canadian Institutes of Health Research
- AMIDEX program of Aix-Marseille Universite
- IRP funds of the NIH
- NIH [GM113172, GM51986]
- European Research Council [DOME-261105, 260787]
- Bettencourt-Schueller Coup d'elan pour la recherche Francaise
- ANR grant IBM [ANR-14-CE09-0025-01]
- ANR grant HiResBacs [ANR-15-CE11-0023]
- France-BioImaging (Investments for the future) [ANR-10-INBS-04]
- Imagine Optic
- European Research Council (ERC) [260787] Funding Source: European Research Council (ERC)
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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.
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