Working strokes by single molecules of the kinesin-related microtubule motor ncd

Abstract

The ncd protein is a dimeric, ATP-powered motor that belongs to the kinesin family of microtubule motor proteins. Here we resolve single mechanochemical cycles of recombinant, dimeric, full-length ncd, using optical-tweezers-based instrumentation and a three-bead, suspended-microtubule assay. Under conditions of limiting ATP, isolated and transient microtubule-binding events exhibit exponentially distributed and ATP-concentration-dependent lifetimes. These events do not involve consecutive steps along the microtubule, quantitatively confirming that ncd is non-processive. At low loads, a single motor molecule produces ATP-triggered working strokes of about 9 nm, which occur at the ends of binding events.

Cite this article

deCastro, M., Fondecave, R., Clarke, L. et al. Working strokes by single molecules of the kinesin-related microtubule motor ncd. Nat Cell Biol 2, 724–729 (2000). https://doi.org/10.1038/35036357

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