Hydrolysis of AMPPNP by the motor domain of ncd, a kinesin-related protein

被引:17
|
作者
Suzuki, Y
Shimizu, T
Morii, H
Tanokura, M
机构
[1] NATL INST BIOSCI & HUMAN TECHNOL,HIGASHI KU,TSUKUBA,IBARAKI 305,JAPAN
[2] UNIV TOKYO,BIOTECHNOL RES CTR,BUNKYO KU,TOKYO 113,JAPAN
[3] NATL INST ADV INTERDISCIPLINARY RES,HIGASHI KU,TSUKUBA,IBARAKI 305,JAPAN
关键词
adenylylimidodiphosphate; Ncd; kinesin; molecular motor; P-31; NMR;
D O I
10.1016/S0014-5793(97)00472-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
AMPPNP was found to be hydrolyzed by the motor domain of ncd (the product of a Drosophila gene, Iron-claret disjunctional), a kinesin-related protein. This hydrolysis could be monitored by P-31 NMR spectroscopy and by an assay of phosphate, one of the products of the hydrolysis. The rate was approximate to 0.00001 s(-1), 1% of the ATP turnover rate, The AMPPNP turnover was not stimulated by microtubules. Kinesin motor domain also turned over AMPPNP but at a somewhat lower rate, Although the turnover was slow, the present finding may present an important caveat, since AMPPNP has been widely used for investigations of kinesin and kinesin-related proteins as a non-hydrolyzable ATP analogue. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:29 / 32
页数:4
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