Journal
JOURNAL OF BIOCHEMISTRY
Volume 149, Issue 5, Pages 539-550Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvr012
Keywords
ATP analogue; kinesin; kinetics; plant; rice
Categories
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [19570047]
- Grants-in-Aid for Scientific Research [19570047, 22380186] Funding Source: KAKEN
Ask authors/readers for more resources
We previously demonstrated that the rice kinesin K16, which belongs to the kinesin-7 subfamily, has unique enzymatic properties and atomic structure within key functional regions. In this study, we focused on a novel rice plant kinesin, K23, which also belongs to the kinesin-7 subfamily. The biochemical characterization of the K23 motor domain (K23MD) was studied and compared with the rice kinesin K16 and other related kinesins. K23 exhibits similar to 45-fold (1.3 Pi mol(-1)site mol(-1)s(-1)) lower microtubule-dependent ATPase activity than conventional kinesins, whereas its affinity for microtubules is comparable with conventional kinesins. MgADP-free K23 is unstable compared with the unusually stable MgADP-free K16MD. The enzymatic properties of K23MD are somewhat different from those of K16. We used a fluorescent ATP analogue 2'(3')-O-(N'-methylanthraniloyl)-ATP (mant-ATP) for the kinetic characterization of K23. The fluorescence of mant-ATP was not significantly altered during its hydrolysis by K23. However, significant fluorescence resonance energy transfer (FRET) between mant-ATP and W21 in the motor domain was observed. The kinetic study using FRET revealed that K23 has unique kinetic characteristics when compared with other kinesins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available