Article abstract
Nature Cell Biology 4, 790 - 797 (2002)
Published online: 23 September 2002 | doi:10.1038/ncb857
Chemomechanical coupling of the forward and backward steps of single kinesin molecules
Masayoshi Nishiyama1,2,7, Hideo Higuchi3,4 & Toshio Yanagida1,5,6
Abstract
The molecular motor kinesin travels processively along a microtubule in a stepwise manner. Here we have studied the chemomechanical coupling of the hydrolysis of ATP to the mechanical work of kinesin by analysing the individual stepwise movements according to the directionality of the movements. Kinesin molecules move primarily in the forward direction and only occasionally in the backward direction. The hydrolysis of a single ATP molecule is coupled to either the forward or the backward movement. This bidirectional movement is well described by a model of Brownian motion assuming an asymmetric potential of activation energy. Thus, the stepwise movement along the microtubule is most probably due to Brownian motion that is biased towards the forward direction by chemical energy stored in ATP molecules.
- Single Molecule Processes Project, ICORP, JST, 2-4-14, Senba-Higashi, Mino, Osaka, 562-0035, Japan
- Department of Biophysical Engineering, Osaka University 1-3, Machikaneyama, Toyonaka, Osaka, 560-8531, Japan
- Department of Metallurgy, Graduate School of Engineering, Tohoku University, Sendai, 980-8579, Japan
- Center of Interdisciplinary Research, Tohoku University, Sendai, 980-8579, Japan
- Department of Physiology and Biosignaling, Graduate School of Medicine, Osaka University, 2-2, Yamadaoka, Suita, Osaka, 565-0871, Japan
- Laboratories for Nanobiology, Graduate School of Frontier Biosciences Osaka University, A4, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan
- Current address: Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto, 606-8502, Japan
Correspondence to: Hideo Higuchi3,4 e-mail: higuchi@material.tohoku.ac.jp
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