Kinesin hydrolyses one ATP per 8-nm step

Mark J. Schnitzer () and Steven M. Block
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Mark J. Schnitzer: Princeton University
Steven M. Block: †Molecular Biology, Princeton University

Nature, 1997, vol. 388, issue 6640, 386-390

Abstract: Abstract Kinesin is a two-headed, ATP-dependent motor protein1,2 that moves along microtubules indiscrete steps3 of 8 nm. In vitro, single molecules produceprocessive movement4,5, motors typically take ∼100steps before releasing from a microtubule5,6,7 . A central question relates tomechanochemical coupling in this enzyme: how many molecules ofATP are consumed per step? For the actomyosin system,experimental approaches to this issue have generated considerablecontroversy8,9. Here we take advantage of theprocessivity of kinesin to determine the coupling ratio withoutrecourse to direct measurements of ATPase activity, which aresubject to large experimental uncertainties8,10,11,12. Beads carrying singlemolecules of kinesin moving on microtubules were tracked with highspatial and temporal resolution by interferometry3,13. Statistical analysis of theintervals between steps at limiting ATP, and studies offluctuations in motor speed as a function of ATPconcentration14,15, allow the coupling ratio to bedetermined. At near-zero load, kinesin moleculeshydrolyse a single ATP molecule per 8-nm advance. Thisfinding excludes various one-to-many andmany-to-one coupling schemes, analogous to thoseadvanced for myosin, and places severe constraints on models for movement.

Date: 1997
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DOI: 10.1038/41111

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