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J. Biol. Chem., Vol. 280, Issue 44, 37048-37060, November 4, 2005

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Alternating Site ATPase Pathway of Rat Conventional Kinesin^*

From the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712

The pathway of ATP hydrolysis by rat kinesin was established by pre-steady-state kinetic methods. A 406-residue long N-terminal fragment was shown by sedimentation equilibrium analysis to form a dimer with a K_d of 46 nM. The pathway of ATP hydrolysis follows the Gilbert-Johnson pathway determined previously for a similarsized N-terminal fragment of Drosophila conventional kinesin. However, the rates of ADP release were at least 3-fold faster, and ATP hydrolysis was 5-fold faster. Paralleling our previous mechanistic data, these results support an alternating site ATPase pathway, including a captive head state as an intermediate in the kinesin ATPase cycle. The kinetic data presented in this report once again point to the importance of the captive head state and argue against a pathway that short-circuits this key intermediate. In addition, several unique aspects of the rat kinesin kinetics reveal new aspects of the ATPase-coupling mechanism. These studies provide a baseline set of kinetic parameters against which future studies of rat kinesin mutants may be evaluated and directly correlated with the structure of the dimeric kinesin.

Received for publication, March 17, 2005 , and in revised form, August 12, 2005.

^* This work was supported by National Institutes of Health Grant GM-26726-25 (to K. A. J.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: University of Texas at Austin, MBB 3.122, 2500 Speedway #A4800, Austin, TX 78735. Tel.: 512-471-0434; Fax: 512-471-0435; E-mail: kajohnson{at}mail.utexas.edu.

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