Document Detail


Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force.
MedLine Citation:
PMID:  21248229     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Beiyan Nan; Jing Chen; John C Neu; Richard M Berry; George Oster; David R Zusman
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-01-19
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  108     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-02-09     Completed Date:  2011-03-30     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2498-503     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cell Biology, and Biophysics Graduate Group, University of California, Berkeley, CA 94720, USA.
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MeSH Terms
Descriptor/Qualifier:
Cytoskeleton / genetics,  metabolism*
Fimbriae, Bacterial / genetics,  metabolism*
Models, Biological*
Myxococcus xanthus / cytology,  genetics,  metabolism*
Periplasmic Proteins / genetics,  metabolism*
Proton-Motive Force / physiology*
Grant Support
ID/Acronym/Agency:
GM20509/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Periplasmic Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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