Single-headed mode of kinesin-5

EMBO Rep. 2008 Aug;9(8):761-5. doi: 10.1038/embor.2008.96. Epub 2008 Jun 13.

Abstract

In most organisms, kinesin-5 motors are essential for mitosis and meiosis, where they crosslink and slide apart the antiparallel microtubule half-spindles. Recently, it was shown using single-molecule optical trapping that a truncated, double-headed human kinesin-5 dimer can step processively along microtubules. However, processivity is limited ( approximately 8 steps) with little coordination between the heads, raising the possibility that kinesin-5 motors might also be able to move by a nonprocessive mechanism. To investigate this, we engineered single-headed kinesin-5 dimers. We show that a set of these single-headed Eg5 dimers drive microtubule sliding at about 90% of wild-type velocity, indicating that Eg5 can slide microtubules by a mechanism in which one head of each Eg5 head-pair is effectively redundant. On the basis of this, we propose a muscle-like model for Eg5-driven microtubule sliding in spindles in which most force-generating events are single-headed interactions and alternate-heads processivity is rare.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Animals
  • Dimerization
  • Electrophoresis, Polyacrylamide Gel
  • Kinesins / chemistry
  • Kinesins / metabolism
  • Kinesins / physiology*
  • Microtubules / physiology*
  • Models, Biological
  • Xenopus Proteins / chemistry
  • Xenopus Proteins / metabolism
  • Xenopus Proteins / physiology*
  • Xenopus laevis

Substances

  • Xenopus Proteins
  • Adenosine Triphosphatases
  • Kinesins