Kinesin heads fused to hinge-free myosin tails drive efficient motility

Verena Eickel, Douglas Drummond, Nick Carter, Andrew Lockhart, John Kendrick Jones, Robert Cross

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

The rat kinesin motor domain was fused at residues 433, 411, 376 or 367, respectively, to the C-terminal 1185, 1187, 1197 or 1185 residues of the brush border myosin tail. In motility assays, K433myt and K411myt, which preserve the head-proximal kinesin hinge, and K367myt, which deletes it, drove rapid microtubule sliding (∼0.6 μms-1) that was optimal when the head-pairs were spaced apart by adding 1:1 headless myosin tails. K376myt, which partially deletes the head-proximal hinge, showed poor motility in sliding assays but wild type processivity, velocity and stall force in single molecule optical trapping. Accordingly, the head-proximal kinesin hinge is functionally dispensable.

Original languageEnglish
Pages (from-to)54-58
Number of pages5
JournalFEBS Letters
Volume569
Issue number1-3
DOIs
Publication statusPublished - Jul 2 2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Kinesin heads fused to hinge-free myosin tails drive efficient motility'. Together they form a unique fingerprint.

Cite this