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Papers In Press, published online ahead of print July 6, 2004
J. Biol. Chem, 10.1074/jbc.M404203200
Submitted on April 15, 2004
Revised on June 21, 2004
Accepted on June 23, 2004

Mechanistic analysis of the mitotic kinesin Eg5

Jared C. Cochran, Christopher A. Sontag, Zoltan Maliga, Tarun M Kapoor, John J. Correia, and Susan P. Gilbert

Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260

Corresponding Author: spg1{at}pitt.edu

Eg5 is a slow, plus-end-directed microtubule-based motor of the BimC kinesin family that is essential for bipolar spindle formation during eukaryotic cell division. We have analyzed two human Eg5/KSP motors, Eg5-367 and Eg5-437, and both are monomeric based on results from sedimentation velocity and sedimentation equilibrium centrifugation as well as analytical gel filtration. The steady-state parameters were Eg5-367: kcat = 5.5 s-1, K1/2,Mt = 0.7 mu M, and Km,ATP = 25 mu M and Eg5-437: kcat = 2.9 s-1, K1/2,Mt = 4.5 mu M, and Km,ATP = 19 mu M. MantATP binding was rapid at 2-3 mu M-1s-1, followed immediately by ATP hydrolysis at 15 s-1. ATP-dependent Mt•Eg5 dissociation was relatively slow and rate-limiting at 8 s-1 with mantADP release at 40 s-1. Surprisingly, Eg5-367 binds microtubules more effectively (11 mu M-1s-1) than Eg5-437 (0.7 mu M-1s-1), consistent with the steady-state K1/2,Mt and the mantADP release K1/2,Mt. These results indicate that the ATPase pathway for monomeric Eg5 is more similar to conventional kinesin than the spindle motors Ncd and Kar3 where ADP product release is rate-limiting for steady-state turnover.


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