Kinesin crouches to sprint but resists pushing.
Recent optical trap experiments have applied resisting, assisting, and sideways loads to conventional kinesin moving on microtubules at fixed [ATP]. To gain insight into intermediate motions when the motor protein takes its 8.2-nm steps, the velocity and randomness data have been analyzed by using discrete-state stochastic models with a three-dimensional "energy landscape." The bead size and tether angle play a crucial role. The analysis implies that on binding ATP the motor "crouches," the point of attachment of the tether at the necklinker junction moving downward toward the microtubule by 0.5-0.7 nm, while inching forward by only 0.1-0.2 nm, before completing the step from a transition state by a unitary "sprint" of approximately 7.8 nm. These inferences accord with high-resolution observations that exclude a previously predicted substep of 1.8-2.1 nm. Assisting and leftward loads are opposed in that the perpendicular component of the tension in the tether is enhanced by approximately 2 pN, which reduces the velocity, but sideways lurching is not supported.
Fisher
Michael E
ME
Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742, USA.
Kim
Young C
YC
D000255:Adenosine Triphosphate / Q000378:metabolism; D055592:Biophysical Phenomena; D001703:Biophysics; D016547:Kinesins / Q000737:chemistry*
D000255:Adenosine Triphosphate; D016547:Kinesins