The mechanism of force transmission at bacterial focal adhesion complexes

Nature. 2016 Nov 24;539(7630):530-535. doi: 10.1038/nature20121. Epub 2016 Oct 5.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Adhesion / physiology*
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Proteins / metabolism*
  • Cell Movement
  • Focal Adhesions / metabolism*
  • Molecular Motor Proteins / metabolism
  • Myxococcus xanthus / cytology
  • Myxococcus xanthus / physiology*
  • Periplasm / metabolism
  • Rotation


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Molecular Motor Proteins