On the hand-over-hand mechanism of kinesin.
We present here a simple theoretical model for conventional kinesin. The model reproduces the hand-over-hand mechanism for kinesin walking to the plus end of a microtubule. A large hindering force induces kinesin to walk slowly to the minus end, again by a hand-over-hand mechanism. Good agreement is obtained between the calculated and experimental results on the external force dependence of the walking speed, the forward/backward step ratio, and dwell times for both forward and backward steps. The model predicts that both forward and backward motions of kinesin take place at the same chemical state of the motor heads, with the front head being occupied by an ATP (or ADP,Pi) and the rear being occupied by an ADP. The direction of motion is a result of the competition between the power stroke produced by the front head and the external load. The other predictions include the external force dependence of the chemomechanical coupling ratio (e.g., the stepping distance/ATP ratio) and the walking speed of kinesin at force ranges that have not been tested by experiments. The model predicts that the chemomechanical coupling remains tight in a large force range. However, when the external force is very large (e.g., approximately 18 pN), kinesin slides in an inchworm fashion, and the translocation of kinesin becomes loosely coupled to ATP turnovers.
Shao
Qiang
Q
Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Gao
Yi Qin
YQ
D000244:Adenosine Diphosphate / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D001703:Biophysics / Q000379:methods*; D004398:Dyneins / Q000737:chemistry; D006868:Hydrolysis; D016547:Kinesins / Q000737:chemistry*; D008954:Models, Biological; D020409:Molecular Motor Proteins
D020409:Molecular Motor Proteins; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D004398:Dyneins; D016547:Kinesins