Pressure-induced changes in the structure and function of the kinesin-microtubule complex.

ABSTRACT: Kinesin-1 is an ATP-driven molecular motor that "walks" along a microtubule by working two heads in a "hand-over-hand" fashion. The stepping motion is well-coordinated by intermolecular interactions between the kinesin head and microtubule, and is sensitively changed by applied forces. We demonstrate that hydrostatic pressure works as an inhibitory action on kinesin motility. We developed a high-pressure microscope that enables the application of hydrostatic pressures of up to 200 MPa (2000 bar). Under high-pressure conditions, taxol-stabilized microtubules were shortened from both ends at the same speed. The sliding velocity of kinesin motors was reversibly changed by pressure, and reached half-maximal value at approximately 100 MPa. The pressure-velocity relationship was very close to th

SUBMITTER: Nishiyama M 

PROVIDER: S-EPMC2716646 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature