Evidence that focal adhesion complexes power bacterial gliding motility. Author Tâm Mignot, Joshua Shaevitz, Patricia Hartzell, David Zusman Publication Year 2007 Type Journal Article 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. Keywords Models, Biological, Recombinant Fusion Proteins, Movement, Bacterial Proteins, Molecular Motor Proteins, Luminescent Proteins, Focal Adhesions, Myxococcus xanthus, Anti-Bacterial Agents, Cephalexin, Bacterial Adhesion, Fimbriae, Bacterial Journal Science Volume 315 Issue 5813 Pages 853-6 Date Published 02/2007 Alternate Journal Science Google ScholarBibTeXEndNote X3 XML