Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.

Myxococcus xanthus is a Gram-negative bacterium that glides over surfaces without the aid of flagella. Two motility systems are used for locomotion: social-motility, powered by the retraction of type IV pili, and adventurous (A)-motility, powered by unknown mechanism(s). We have shown that AgmU, an...

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Main Authors: Nan, B, Chen, J, Neu, J, Berry, R, Oster, G, Zusman, DR
格式: Journal article
语言:English
出版: 2011
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author Nan, B
Chen, J
Neu, J
Berry, R
Oster, G
Zusman, DR
author_facet Nan, B
Chen, J
Neu, J
Berry, R
Oster, G
Zusman, DR
author_sort Nan, B
collection OXFORD
description Myxococcus xanthus is a Gram-negative bacterium that glides over surfaces without the aid of flagella. Two motility systems are used for locomotion: social-motility, powered by the retraction of type IV pili, and adventurous (A)-motility, powered by unknown mechanism(s). We have shown that AgmU, an A-motility protein, is part of a multiprotein complex that spans the inner membrane and periplasm of M. xanthus. In this paper, we present evidence that periplasmic AgmU decorates a looped continuous helix that rotates clockwise as cells glide forward, reversing its rotation when cells reverse polarity. Inhibitor studies showed that the AgmU helix rotation is driven by proton motive force (PMF) and depends on actin-like MreB cytoskeletal filaments. The AgmU motility complex was found to interact with MotAB homologs. Our data are consistent with a mechanochemical model in which PMF-driven motors, similar to bacterial flagella stator complexes, run along an endless looped helical track, driving rotation of the track; deformation of the cell surface by the AgmU-associated proteins creates pressure waves in the slime, pushing cells forward.
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spelling oxford-uuid:91c79711-88a1-4e29-b4b7-2ef06d4ac09b2022-03-26T23:20:56ZMyxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:91c79711-88a1-4e29-b4b7-2ef06d4ac09bEnglishSymplectic Elements at Oxford2011Nan, BChen, JNeu, JBerry, ROster, GZusman, DRMyxococcus xanthus is a Gram-negative bacterium that glides over surfaces without the aid of flagella. Two motility systems are used for locomotion: social-motility, powered by the retraction of type IV pili, and adventurous (A)-motility, powered by unknown mechanism(s). We have shown that AgmU, an A-motility protein, is part of a multiprotein complex that spans the inner membrane and periplasm of M. xanthus. In this paper, we present evidence that periplasmic AgmU decorates a looped continuous helix that rotates clockwise as cells glide forward, reversing its rotation when cells reverse polarity. Inhibitor studies showed that the AgmU helix rotation is driven by proton motive force (PMF) and depends on actin-like MreB cytoskeletal filaments. The AgmU motility complex was found to interact with MotAB homologs. Our data are consistent with a mechanochemical model in which PMF-driven motors, similar to bacterial flagella stator complexes, run along an endless looped helical track, driving rotation of the track; deformation of the cell surface by the AgmU-associated proteins creates pressure waves in the slime, pushing cells forward.
spellingShingle Nan, B
Chen, J
Neu, J
Berry, R
Oster, G
Zusman, DR
Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.
title Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.
title_full Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.
title_fullStr Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.
title_full_unstemmed Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.
title_short Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.
title_sort myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force
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