Processivity of single-headed kinesin motors

被引:15
作者
Xie, Ping [1 ]
Dou, Shuo-Xing [1 ]
Wang, Peng-Ye [1 ]
机构
[1] Chinese Acad Sci, Inst Phys, Lab Soft Matter Phys, Beijing 100080, Peoples R China
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2007年 / 1767卷 / 12期
基金
中国国家自然科学基金;
关键词
kinesin; processivity; mechanochemistry; microtubule; molecular motor;
D O I
10.1016/j.bbabio.2007.09.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2007 Elsevier B.V.All rights reserved.
引用
收藏
页码:1418 / 1427
页数:10
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