Characterization of a novel rice kinesin O12 with a calponin homology domain.

Nozomi Umezu, Nobuhisa Umeki, Toshiaki Mitsui, Kazunori Kondo, Shinsaku Maruta

Journal of biochemistry 2011 Jan

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Genomic analysis predicted that the rice (Oryza sativa var. japonica) genome encodes at least 41 kinesin-like proteins including the novel kinesin O12, which is classified as a kinesin-14 family member. O12 has a calponin homology (CH) domain that is known as an actin-binding domain. In this study, we expressed the functional domains of O12 in Escherichia coli and determined its enzymatic characteristics compared with other kinesins. The microtubule-dependent ATPase activity of recombinant O12 containing the motor and CH domains was significantly reduced in the presence of actin. Interestingly, microtubule-dependent ATPase activity of the motor domain was also affected by actin in the absence of the CH domain. Our findings suggest that the motor activity of the rice plant-specific kinesin O12 may be regulated by actin.

Citation

Nozomi Umezu, Nobuhisa Umeki, Toshiaki Mitsui, Kazunori Kondo, Shinsaku Maruta. Characterization of a novel rice kinesin O12 with a calponin homology domain. Journal of biochemistry. 2011 Jan;149(1):91-101