The mechanism of force transmission at bacterial focal adhesion complexes View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-10-05

AUTHORS

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, Tâm Mignot

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. More... »

PAGES

530-535

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature20121

DOI

http://dx.doi.org/10.1038/nature20121

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000397505

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27749817


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19 schema:description 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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28 absence
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30 activity
31 adhesion complexes
32 adhesion proteins
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35 axis
36 bacteria
37 bacterial focal adhesion complexes
38 bacterial gliding motility
39 cells
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43 contractile activity
44 cyclic interaction
45 deltaproteobacterium Myxococcus xanthus
46 flagella
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49 force transmission
50 gliding motility
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52 handed helical path
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55 interaction
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57 left-handed rotation
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59 machinery
60 mechanism
61 membrane
62 model
63 molecular model
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65 motility
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74 pili
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76 point
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