Abstract
Coupling between ATP hydrolysis and microtubule movement was demonstrated several years ago in flagellar axonemes1,2 and subsequent studies suggest that the relevant microtubule motor, dynein, uses ATP to drive microtubule sliding by a cross-bridge mechanism analogous to that of myosin in muscles3,4. Kinesin5, a microtubule-based motility protein which may participate in organelle transport and mitosis6, binds microtubules in a nucleo-tide-sensitive manner5,7,8, and requires hydrolysable nucleotides to translocate microtubules over a glass surface9,10. Recently, neuronal kinesin was shown to possess microtubule-activated ATPase activity11,12 although coupling between ATP hydrolysis and motility was not demonstrated. Here we report that sea urchin egg kinesin, prepared either with or without a 5′-adenylyl imido-diphosphate(AMPPNP)-induced microtubule binding step, also possesses significant microtubule-activated ATPase activity when Mg-ATP is used as a substrate. This ATPase activity is inhibited in a dose-dependent manner by addition of Mg-free ATP, by chelation of Mg2+ with EDTA, by addition of Na3VO4, or by addition of AMPPNP with or without Mg2+ Addition of these same reagents also inhibits the microtubule-translocating activities of sea urchin egg kinesin in a dose-dependent manner, supporting the hypothesis that kinesin-driven motility is coupled to the microtubule-activated Mg2+-ATPase activity.
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References
1. Gibbons, B. H. & Gibbons, I. R. /. Cell Biol 54, 75–97 (1972). 2. Brokaw, C. J. & Benedict, B. Archs Biochem. Biophys. 125, 770–778 (1968). 3. Gibbons, I. R. /. Cell Biol. 91, 107s–124s (1981). 4. Johnson, K. A. A. Rev. Biophys. biophys. Chem. 14, 161–188 (1985). 5. Vale, R. D., Reese, T. S. & Sheetz, M. P. Cell 42, 39–50 (1985). 6. Vale, R. D., Scholey, J. M. & Sheetz, M. P. Trends biochem. Sci. 11, 464–468 (1986). 7. Vale, R. D., Schnapp, B. J., Sheetz, M. P. & Reese, T. S. /. Cell Biol. 103, 552a (1986). 8. Scholey, J. M., Porter, M. E., Grissom, P. M. & Mclntosh, J. R. Nature 318,483–486 (1985). 9. Schnapp, B. J., Kahn, S., Sheetz, M. P., Vale, R. D. & Reese, T. S. J. Cell Biol. 103,551a (1986). 10. Porter, M. E. et al. J. biol. Chem. 262, 2794–2802 (1987). 11. Kuznetsov, S. A. & Gelfand, V. I. Proc. natn. Acad. Sci. U.S.A. 83, 8530–8534 (1986). 12. Bloom, G. S., Wagner, M. C. & Brady, S. T. /. biol. Chem. (submitted). 13. Adelstein, R. S., Pato, M. D., Sellers, J. R., de Lanerolle, P. & Conti, M. A. in Basic Biology of Muscles: A Comparative Approach (eds Twarog, B. M., Levine, R. J. C. & Dewey, M. M.) 273–281 (Raven, New York, 1982). 14. Sellers, J. R., Spudich, J. A. & Sheetz, M. P. J. Cell Biol. 101, 1897–1902 (1985). 15. Suprenant, K. A. & Marsh, J. C. /. Cell Sci. 87, 71–84 (1987) 16. Hayashi, M. Archs Biochem. Biophys. 165, 288–296 (1974). 17. Brady, S. T. Nature 317, 73–75 (1985). 18. Penningroth, S. M., Rose, P. M. & Peterson, D. D. J. Cell Biol. 103, 552a (1986). 19. Scholey, J. M., Neighbors, B., Mclntosh, J. R. & Salmon, E. D. /. biol. Chem. 259,6516–6525 (1984). 20. Dinenberg, A. S., Mclntosh, J. R. & Scholey, J. M. Ann. N. Y. Acad. Sci. 466,431–435 (1986). 21. Pratt, M. M. Int. Rev. Cytol. 87, 83–105 (1984). 22. Collins, C. A. & Vallee, R. B. Proc. natn. Acad. Sci. U.S.A. 83, 4799–4803 (1986). 23. Williams, R. C. Jr & Lee, J. C. Meth. Enzym. 85, 376–385 (1982). 24. Amos, L. A. /. Cell Sci. 87, 105–111 (1987). 25. Vallee, R. B. & Bloom, G. S. Proc. natn. Acad. Sci. U.S.A. 80, 6259–6263 (1983). 26. Seals, J. R., McDonald, J. M., Brims, D. & Jarett, L. Analyt. Biochem. 90, 785–795 (1978). 27. Goodno, C. C. Meth. Enzym. 85, 116–123 (1982).
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Cohn, S., Ingold, A. & Scholey, J. Correlation between the ATPase and microtubule translocating activities of sea urchin egg kinesin. Nature 328, 160–163 (1987). https://doi.org/10.1038/328160a0
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DOI: https://doi.org/10.1038/328160a0
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