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J Biol Chem, Vol. 274, Issue 6, 3667-3671, February 5, 1999
From the Department of Physiology and Biophysics, University of
Washington, Seattle, Washington 98195-7290
Conventional kinesin is a motor protein that
moves stepwise along microtubules carrying membrane-bound organelles
toward the periphery of cells. The steps are of amplitude 8.1 nm, the
distance between adjacent tubulin binding sites, and are powered by the hydrolysis of ATP. We have asked: how many steps does kinesin take for
each molecule of ATP that it hydrolyzes? To answer this question, the
motility and ATP hydrolysis of recombinant, heterotetrameric and
homodimeric conventional Drosophila kinesins adsorbed to
200-nm-diameter casein-coated silica beads were assayed under
identical, single-molecule conditions. Division of the speed by the
maximum microtubule-activated ATPase rate gave a stoichiometry of
1.08 ± 0.09 steps for each ATP hydrolyzed at 1 mM
ATP. Therefore, under low loads in which the drag force 
1 pN,
coupling between the chemical and mechanical cycles of kinesin is
tight, consistent with conventional power stroke models. Our results
rule out models that require two or more ATPs/step, such as some
thermal ratchet models, or that propose multiple steps powered by
single ATPs.
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