NOVEL HETEROTRIMERIC KINESIN-RELATED PROTEIN PURIFIED FROM SEA-URCHIN EGGS

被引：228

作者：

COLE, DG ^{[1
]}

CHINN, SW ^{[1
]}

WEDAMAN, KP ^{[1
]}

HALL, K ^{[1
]}

VUONG, T ^{[1
]}

SCHOLEY, JM ^{[1
]}

机构：

[1] UNIV CALIF DAVIS,DIV BIOL SCI,MOLEC & CELLULAR BIOL SECT,DAVIS,CA 95616

来源：

NATURE | 1993年 / 366卷 / 6452期

关键词：

D O I：

10.1038/366268a0

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：

KINESIN heavy chain and kinesin-related polypeptides (KRPs) comprise a family of motor proteins with diverse intracellular transport functions1-7. Using pan-kinesin peptide antibodies that react with these proteins8,9, we have previously purified from sea urchin eggs a trimeric microtubule-binding and bundling protein, KRP(85/95) (ref. 8) comprising subunits of M(r) 115,000 (115K), 95K and 85K. We report here that kinesin-related genes encode the 85K and 95K subunits, and that the protein can be immunoprecipitated from cytosol as a trimeric complex using an 85K monoclonal antibody. We also find that purified KRP(85/95) directs movements towards the 'plus' ends of microtubules. To our knowledge, this protein is the first kinesin-related motor to be purified from its natural host cell in a native multimeric state.

引用

页码：268 / 270

页数：3

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