Journal
NATURE CELL BIOLOGY
Volume 2, Issue 10, Pages 724-729Publisher
MACMILLAN PUBLISHERS LTD
DOI: 10.1038/35036357
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Funding
- NIGMS NIH HHS [1R55GM55679-01] Funding Source: Medline
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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.
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