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Genetic engineering of a Ca 2+ dependent chemical switch into the linear biomotor kinesin
Author(s) -
Konishi Kaoru,
Uyeda Taro Q.P.,
Kubo Tai
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.05.037
Subject(s) - kinesin , calmodulin , microtubule , chemistry , motor protein , atp hydrolysis , biophysics , microbiology and biotechnology , binding site , atpase , biochemistry , enzyme , biology
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 Ca 2+ ‐calmodulin, the association of the engineered kinesin with microtubules showed a steep Ca 2+ ‐dependency in ATPase activity at Ca 2+ concentrations of pCa 6.5–8. The calmodulin‐binding domain of plant kinesin‐like calmodulin‐binding protein is also known to confer Ca 2+ ‐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., Ca 2+ ‐calmodulin) and, thus, can be used as a model system for a bio/nano‐actuator.