Bidirectional motility of the fission yeast kinesin-5, Cut7

Biochem Biophys Res Commun. 2014 Mar 28;446(1):231-4. doi: 10.1016/j.bbrc.2014.02.106. Epub 2014 Feb 28.

Abstract

Kinesin-5 is a homotetrameric motor with its motor domain at the N-terminus. Kinesin-5 crosslinks microtubules and functions in separating spindle poles during mitosis. In this study, the motile properties of Cut7, fission yeast kinesin-5, were examined for the first time. In in vitro motility assays, full-length Cut7 moved toward minus-end of microtubules, but the N-terminal half of Cut7 moved toward the opposite direction. Furthermore, additional truncated constructs lacking the N-terminal or C-terminal regions, but still contained the motor domain, did not switch the motile direction. These indicated that Cut7 was a bidirectional motor, and microtubule binding regions at the N-terminus and C-terminus were not involved in its directionality.

Keywords: Cell cycle; Cut7; Fission yeast; Kinesin; Microtubule; Spindle.

MeSH terms

  • Binding Sites
  • Cell Division
  • Kinesin / chemistry
  • Kinesin / genetics
  • Kinesin / metabolism*
  • Microtubules / metabolism
  • Movement
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Schizosaccharomyces / cytology
  • Schizosaccharomyces / genetics
  • Schizosaccharomyces / metabolism
  • Schizosaccharomyces pombe Proteins / chemistry
  • Schizosaccharomyces pombe Proteins / genetics
  • Schizosaccharomyces pombe Proteins / metabolism*

Substances

  • Cut7 protein, S pombe
  • Peptide Fragments
  • Recombinant Proteins
  • Schizosaccharomyces pombe Proteins
  • Kinesin