The ATPase pathway that drives the kinesin-14 Kar3Vik1 powerstroke

Abstract

Background: Kar3Vik1 binds side-by-side microtubule protofilaments and utilizes a minus-end-directed powerstroke. Results: Microtubule collision occurs through Vik1 followed by Kar3 binding and ADP release, which destabilize Vik1 and generate the intermediate poised for ATP binding. Conclusion: The transient Kar3Vik1 two-head-bound state intermediate was identified. Significance: This study provides new insights into force generation by kinesin-14 motors. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.