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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-10

AUTHORS

Michael J. deCastro, Regis M. Fondecave, Leigh A. Clarke, Christoph F. Schmidt, Russell J. Stewart

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. More... »

PAGES

ncb1000_724

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/35036357

DOI

http://dx.doi.org/10.1038/35036357

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013218447

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11025663


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50 schema:description 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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