Drosophila kinesin: characterization of microtubule motility and ATPase.

W. M. Saxton, M. E. Porter, S. A. Cohn, J. M. Scholey, E. C. Raff, J. R. McIntosh

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83 Scopus citations

Abstract

Preparations of kinesin, a microtubule-based force-producing protein, have been isolated from Drosophila melanogaster embryos by incubation of microtubules with a nonhydrolyzable ATP analogue and gel filtration of proteins released from the microtubules by ATP. These preparations induced MgATP-dependent microtubule gliding in vitro with a Km for MgATP of 44 microM and a Vmax for gliding of 0.9 micron/sec. Samples of Drosophila proteins that were active in motility assays possessed an average ATPase activity in solution of 17 nmol/min per mg that increased to an average of 106 nmol/min per mg in the presence of microtubules. The major polypeptides that copurified with these activities showed relative molecular masses of 115 kDa and 58 kDa. An antiserum raised against the 115-kDa polypeptide also recognized the 110-kDa component of squid kinesin preparations and the 130-kDa component of sea urchin kinesin preparations.

Original languageEnglish (US)
Pages (from-to)1109-1113
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number4
StatePublished - Feb 1988
Externally publishedYes

ASJC Scopus subject areas

  • General
  • Genetics

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    Saxton, W. M., Porter, M. E., Cohn, S. A., Scholey, J. M., Raff, E. C., & McIntosh, J. R. (1988). Drosophila kinesin: characterization of microtubule motility and ATPase. Proceedings of the National Academy of Sciences of the United States of America, 85(4), 1109-1113.