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Biased Binding of Single Molecules and Continuous Movement of Multiple Molecules of Truncated Single-Headed Kinesin

Takashi Kamei ^*, Seiji Kakuta ^* and Hideo Higuchi ^* 

^* Department of Metallurgy, School of Engineering, Tohoku University, Sendai 980-8579, Japan; and Center for Interdisciplinary Research and Biomedical and Engineering Research Organization, Tohoku University, Sendai, Miyagi 980-8578, Japan

Correspondence: Address reprint requests to Hideo Higuchi, Center for Interdisciplinary Research, Tohoku University, Aramaki-aza-aoba, Aoba-ku, Sendai, Miyagi 980-8579, Japan, Tel.: 81-22-217-4735; Fax: 81-22-217-7810; E-mail: higuchi{at}material.tohoku.ac.jp.

Conventional kinesin has a double-headed structure consisting of two motor domains and moves processively along a microtubule using the two heads cooperatively. The movement of single and multiple truncated heads of Drosophila kinesin was measured using a laser trap and nanometer detecting apparatus. Single molecules of single-headed kinesin bound to the microtubules with a 3.5 nm biased displacement toward the plus end of the microtubule. The position of these single-headed kinesin molecules bound to a microtubule did not change until they had dissociated, indicating that single kinesin heads utilize nonprocessive movement processes. Two molecules of single-headed kinesin moved continuously along a microtubule with a lower velocity and force than that of single molecules of double-headed kinesin. The biased binding of the heads determines the directionality of movement, whereas two molecules of single-headed kinesin move continuously without dissociation from a microtubule.

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