Working strokes by single molecules of the kinesin-related microtubule motor ncd |
| |
Authors: | deCastro M J Fondecave R M Clarke L A Schmidt C F Stewart R J |
| |
Affiliation: | Department of Bioengineering, University of Utah, Salt Lake City, Utah 84112, USA. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|