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Novel heterotrimeric kinesin-related protein purified from sea urchin eggs

Naturevolume 366pages268270 (1993) | Download Citation

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Abstract

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 haven previously purified from sea urchin eggs a trimeric microtubule-binding and bundling protein, KRP(85/95) (ref. 8) comprising subunits of Mr115,000 (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.

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  1. Section of Molecular and Cellular Biology, Division of Biological Sciences, University of California, Davis, California, 95616, USA

    • D. G. Cole
    • , S. W. Chinn
    • , K. P. Wedaman
    • , K. Hall
    • , T. Vuong
    •  & J. M. Scholey

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https://doi.org/10.1038/366268a0

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