Genetic engineering of a Ca2+ dependent chemical switch into the linear biomotor kinesin

Kaoru Konishi, Taro Q.P. Uyeda*, Tai Kubo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


Kinesin is a linear motor protein driven by energy released by ATP hydrolysis. In the present work, we genetically installed an M13 peptide sequence into Loop 12 of kinesin, which is one of the major microtubule binding regions of the protein. Because the M13 sequence has high affinity for Ca2+-calmodulin, the association of the engineered kinesin with microtubules showed a steep Ca2+-dependency in ATPase activity at Ca2+ concentrations of pCa 6.5-8. The calmodulin-binding domain of plant kinesin-like calmodulin-binding protein is also known to confer Ca2+-calmodulin regulation to kinesins. Unlike this plant kinesin, however, our novel engineered kinesin achieves this regulation while maintaining the interaction between kinesin and microtubules. The engineered kinesin is switched on/off reversibly by an external signal (i.e., Ca2+-calmodulin) and, thus, can be used as a model system for a bio/nano-actuator.

Original languageEnglish
Pages (from-to)3589-3594
Number of pages6
JournalFEBS Letters
Issue number15
Publication statusPublished - 2006 Jun 26
Externally publishedYes


  • Calmodulin
  • Chemical switch
  • Kinesin
  • M13 peptide
  • Microtubules
  • Motor protein

ASJC Scopus subject areas

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


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