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Tubulin Structure and Nucleotide Binding

  • Eva-Maria Mandelkow
  • Klaus Linse
  • Eckhard Mandelkow

Abstract

In this report we summarize our recent studies to identify the GTP binding site of tubulin, the subunit of microtubules, using the method of direct photoaffinity labeling. We compare the results with predictions derived from a comparison of tubulin with other nucleotide binding proteins. The binding site of the base (peptide 63–77) is consistent with that of other GTP binding proteins; however, its position relative to other presumptive sites (e.g. the phosphate binding loop) differs from the consensus pattern of G-proteins. This means that tubulin represents a distinct class of nucleotide binding proteins.

Keywords

Tryptic Peptide Consensus Pattern Base Binding Presumptive Site Subtilisin Type 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Carroll, S., McCloskey, J., Crain, P., Oppenheimer, N., Marschner, T. and Collier, R.(1985). Proc. Natl. Acad. Sci. U.S.A. 82, 7237–7241.PubMedCrossRefGoogle Scholar
  2. Dever, T.E., Glynias, M J. and Merrick, W.C. (1987). Proc. Natl. Acad. Sci. U.S.A. 84, 1814–1818.PubMedCrossRefGoogle Scholar
  3. De Vos, A., Tong, L., Milburn, M., Matias, P., Jancarik, J., Noguchi, S., Nishimura, S., Miura, K., Ohtsuka, E. and Kim, S.-H. (1988). Science 239, 888–893.PubMedCrossRefGoogle Scholar
  4. Geahlen, R.L. and Haley, B.E. (1977). Proc. Natl. Acad. Sci. U.S.A.74, 4375–4377.PubMedCrossRefGoogle Scholar
  5. Halliday, K.(1984). J. Cyc. Nucl. and Prot. Phosphor. Res. 9, 435–448.Google Scholar
  6. Jurnak, F. (1985). Science 230, 32–36.PubMedCrossRefGoogle Scholar
  7. Krauhs, E., Little, M., Kempf, T., Hofer-Warbinek, R., Ade, W. and Ponstingl, H.(1981). Proc. Natl. Acad. Sci. U.S.A. 78, 4156–4160.PubMedCrossRefGoogle Scholar
  8. La Cour, T.F.M., Nyborg, J., Thirup, S. and Clark, B.F.C. (1985). EMBO J. 4,2385–2388.PubMedGoogle Scholar
  9. Leberman, R. and Egner, U. (1984). EMBO J.3, 339–341.PubMedGoogle Scholar
  10. Linse, K. and Mandelkow, E.-M. (1986). J. Cell Biol. 103, 545a:CrossRefGoogle Scholar
  11. Linse, K. and Mandelkow, E.-M. (1988). J. Biol. Chem.263.Google Scholar
  12. Linse, K. (1988). Ph.D. Thesis, University of Hamburg.Google Scholar
  13. Mandelkow, E.-M., Herrmann, M. and Ruhl, U. (1985). J. Mol. Biol.185, 311–327.PubMedCrossRefGoogle Scholar
  14. Maruta, H. and Korn, E.D. (1981). J. Biol. Chem. 256, 499–502.PubMedGoogle Scholar
  15. Matsudaira, P., Jakes, R., Cameron, L. and Atherton, E. (1985). Proc. Natl. Acad. Sci. U.S.A. 82, 6788–6792.PubMedCrossRefGoogle Scholar
  16. Nath, J.P. and Himes, R. H. (1986). Biochem. Biophys. Res. Comm. 135,1135–1143.PubMedCrossRefGoogle Scholar
  17. Sternberg, M. and Taylor, W. (1984). FEBS Letters175,387–392.PubMedCrossRefGoogle Scholar
  18. Sternlicht, H., Yaffe, M. and Farr, G.(1987). FEBS Letters 214, 226–235.PubMedCrossRefGoogle Scholar
  19. Wierenga, R.K. and Hol, W.G.J. (1983). Nature 302,842–844.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Eva-Maria Mandelkow
    • 1
  • Klaus Linse
    • 1
  • Eckhard Mandelkow
    • 1
  1. 1.Max-Planck-Unit for Structural Molecular BiologyHamburg 52Germany

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