NOVEL HETEROTRIMERIC KINESIN-RELATED PROTEIN PURIFIED FROM SEA-URCHIN EGGS
NOVEL HETEROTRIMERIC KINESIN-RELATED PROTEIN PURIFIED FROM SEA-URCHIN EGGS
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DOI:
10.1038/366268a0
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发表时间:
1993-11-18
期刊:
影响因子:
64.8
通讯作者:
SCHOLEY, JM
中科院分区:
文献类型:
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作者:
COLE, DG;CHINN, SW;SCHOLEY, JM
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.