Evidence that focal adhesion complexes power bacterial gliding motility

Science. 2007 Feb 9;315(5813):853-6. doi: 10.1126/science.1137223.

Abstract

The bacterium Myxococcus xanthus has two motility systems: S motility, which is powered by type IV pilus retraction, and A motility, which is powered by unknown mechanism(s). We found that A motility involved transient adhesion complexes that remained at fixed positions relative to the substratum as cells moved forward. Complexes assembled at leading cell poles and dispersed at the rear of the cells. When cells reversed direction, the A-motility clusters relocalized to the new leading poles together with S-motility proteins. The Frz chemosensory system coordinated the two motility systems. The dynamics of protein cluster localization suggest that intracellular motors and force transmission by dynamic focal adhesions can power bacterial motility.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Bacterial Adhesion*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / physiology*
  • Cephalexin / pharmacology
  • Fimbriae, Bacterial / physiology
  • Focal Adhesions / physiology*
  • Luminescent Proteins
  • Models, Biological
  • Molecular Motor Proteins / analysis
  • Molecular Motor Proteins / genetics
  • Molecular Motor Proteins / physiology*
  • Movement
  • Myxococcus xanthus / cytology
  • Myxococcus xanthus / genetics
  • Myxococcus xanthus / physiology*
  • Recombinant Fusion Proteins / analysis

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • FrzS protein, Myxococcus xanthus
  • Luminescent Proteins
  • Molecular Motor Proteins
  • Recombinant Fusion Proteins
  • yellow fluorescent protein, Bacteria
  • Cephalexin