DIRECTION OF MICROTUBULE MOVEMENT IS AN INTRINSIC PROPERTY OF THE MOTOR DOMAINS OF KINESIN HEAVY-CHAIN AND DROSOPHILA NCD PROTEIN

被引:149
作者
STEWART, RJ [1 ]
THALER, JP [1 ]
GOLDSTEIN, LSB [1 ]
机构
[1] HARVARD UNIV, DEPT CELLULAR & DEV BIOL, 16 DIVIN AVE, CAMBRIDGE, MA 02138 USA
关键词
D O I
10.1073/pnas.90.11.5209
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The kinesin heavy chain and the ncd (non-claret disjunctional) gene product of Drosophila are microtubule-associated motor proteins related by sequence similarity within an almost-equal-to 340-aa domain. Despite the sequence similarity, the kinesin heavy chain and ncd protein move in opposite directions on microtubules. To investigate the molecular basis for direction of movement, we created a series of truncated kinesin heavy chain and ncd proteins. We found that the conserved domain of both proteins has microtubule motor activity, although the efficiency with which ATP hydrolysis is coupled to microtubule movement declines dramatically with increasing truncation. Further, the direction of movement is intrinsic to the conserved motor domains, rather than being a consequence of domain organization or adjacent sequences.
引用
收藏
页码:5209 / 5213
页数:5
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