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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • deCastro, MJ; Fondecave, RM; Clarke, LA; Schmidt, CF; Stewart, RJ

Published Date

  • October 2000

Published In

Volume / Issue

  • 2 / 10

Start / End Page

  • 724 - 729

PubMed ID

  • 11025663

Pubmed Central ID

  • 11025663

Electronic International Standard Serial Number (EISSN)

  • 1476-4679

International Standard Serial Number (ISSN)

  • 1465-7392

Digital Object Identifier (DOI)

  • 10.1038/35036357

Language

  • eng