Processivity of single-headed kinesin motors.
The processive movement of single-headed kinesins is studied by using a ratchet model of non-Markov process, which is built on the experimental evidence that the strong binding of kinesin to microtubule in rigor state induces a large apparent change in the local microtubule conformation. In the model, the microtubule plays a crucial active role in the kinesin movement, in contrast to the previous belief that the microtubule only acts as a passive track for the kinesin motility. The unidirectional movement of single-headed kinesin is resulted from the asymmetric periodic potential between kinesin and microtubule while its processivity is determined by its binding affinity for microtubule in the weak ADP state. Using the model, various experimental results for monomeric kinesin KIF1A, such as the mean step size, the step-size distribution, the long run length and the mean velocity versus load, can be well explained quantitatively. This local conformational change of the microtubule may also play important roles in the processive movement of conventional two-headed kinesins. An experiment to verify the model is suggested.
Xie
Ping
P
Department of Physics, Renmin University of China, Beijing 100872, China. pxie@aphy.iphy.ac.cn
Dou
Shuo-Xing
SX
Wang
Peng-Ye
PY
D000818:Animals; D006801:Humans; D016547:Kinesins / Q000502:physiology*; D008870:Microtubules / Q000502:physiology; D008954:Models, Biological; D008956:Models, Chemical; D009068:Movement / Q000502:physiology; D014404:Tubulin / Q000378:metabolism
D014404:Tubulin; D016547:Kinesins