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

Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1756-2651 (Electronic) Linking ISSN: 0021924X NLM ISO Abbreviation: J Biochem Subsets: MEDLINE

Publication: : Abingdon, UK : Oxford University Press
Original Publication: Tokyo : Japanese Biochemical Society

Oryza*; Kinesins/*chemistry ; Plant Proteins/*chemistry ; Recombinant Proteins/*chemistry; Actins/chemistry ; Adenosine Diphosphate/chemistry ; Adenosine Triphosphatases/chemistry ; Adenosine Triphosphate/chemistry ; Calcium-Binding Proteins/genetics ; Kinesins/classification ; Kinesins/genetics ; Microfilament Proteins/genetics ; Models, Molecular ; Phylogeny ; Plant Proteins/genetics ; Protein Binding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/genetics ; Sequence Homology, Amino Acid ; Calponins

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.

Comment in: J Biochem. 2012 Aug;152(2):207-8. (PMID: 22843988)

0 (Actins)
0 (Calcium-Binding Proteins)
0 (Microfilament Proteins)
0 (Plant Proteins)
0 (Recombinant Proteins)
61D2G4IYVH (Adenosine Diphosphate)
8L70Q75FXE (Adenosine Triphosphate)
EC 3.6.1.- (Adenosine Triphosphatases)
EC 3.6.4.4 (Kinesins)

Date Created: 20101105 Date Completed: 20110505 Latest Revision: 20231213

20231215

10.1093/jb/mvq122

21047815