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Solution structure of a dynein motor domain associated light chain

Nature Structural Biology volume 7, pages 575–579 (2000)Cite this article

Abstract

Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the γ heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six β-β-α motifs. This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a hydrophobic surface within the repeat region that is proposed to interact with the dynein heavy chain. The position of the C-terminal domain on LC1 and the unexpected structural similarity between LC1 and U2A′ from the human spliceosome suggest that this domain interacts with the dynein motor domain.

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Figure 1: Sequence comparison and topology of LC1.
Figure 2: The NMR solution structure of LC1.
Figure 3: Electrostatic surface of LC1 and proposed heavy chain binding site.
Figure 4: LC1 interactions and architecture of the outer dynein arm.

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References

  1. Karki, S. & Holzbaur, E.L. Curr. Opin. Cell Biol. 11, 45–53 (1999).

    Article  CAS  PubMed  Google Scholar 

  2. Mitchell, D.R. Int. Rev. Cytol. 155, 141–180 (1994).

    Article  CAS  PubMed  Google Scholar 

  3. Supp, D.M., Witte, D.P., Potter, S.S. & Brueckner, M. Nature 389, 963–966 (1997).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. King, S.M. Biochim. Biophys. Acta 1496, 60–75 (2000).

    Article  CAS  PubMed  Google Scholar 

  5. Neuwald, A.F., Aravind, L., Spouge, J.L. & Koonin, E.V. Genome Res. 9, 27–43 (1999).

    CAS  PubMed  Google Scholar 

  6. Mocz, G., Helms, M.K., Jameson, D.M. & Gibbons, I.R. Biochemistry 37, 9862–9869 (1998).

    Article  CAS  PubMed  Google Scholar 

  7. Wilkerson, C.G. & Witman, G.B. Mol. Biol. Cell 6, 33a (1995).

    Google Scholar 

  8. Ogawa, K. Nature 352, 643–645 (1991).

    Article  CAS  PubMed  Google Scholar 

  9. Gibbons, I.R., Gibbons, B.H., Mocz, G. & Asai, D.J. Nature 352, 640–643 (1991).

    Article  CAS  PubMed  Google Scholar 

  10. Gee, M.A., Heuser, J.E. & Vallee, R.B. Nature 390, 636–639 (1997).

    Article  CAS  PubMed  Google Scholar 

  11. Samso, M., Radermacher, M., Frank, J. & Koonce, M.P. J. Mol. Biol. 276, 927–937 (1998).

    Article  CAS  PubMed  Google Scholar 

  12. Witman, G.B., King, S.M., Moss, A.G. & Wilkerson, C.G. In Comparative spermatology 20 years after. (ed., Baccetti, B.) 439–443 (Raven Press, New York; 1991).

    Google Scholar 

  13. Pfister, K.K., Fay, R.B. & Witman, G.B. Cell Motil. 2, 525–547 (1982).

    Article  CAS  PubMed  Google Scholar 

  14. Wilkerson, C.G., King, S.M. & Witman, G.B. J. Cell Sci. 107, 497–506 (1994).

    CAS  PubMed  Google Scholar 

  15. Rupp, G., O'Toole, E., Gardner, L.C., Mitchell, B.F. & Porter, M.E. J. Cell Biol. 135, 1853–1865 (1996).

    Article  CAS  PubMed  Google Scholar 

  16. King, S.M. & Patel-King, R.S. J. Cell Sci. 108, 3757–3764 (1995).

    CAS  PubMed  Google Scholar 

  17. Benashski, S.E., Patel-King, R.S. & King, S.M. Biochemistry 38, 7253–7264 (1999).

    Article  CAS  PubMed  Google Scholar 

  18. Kobe, B. & Deisenhofer, J. Trends Biochem. Sci. 19, 415–421 (1994).

    Article  CAS  PubMed  Google Scholar 

  19. Kajava, A.V. J. Mol. Biol. 277, 519–527 (1998).

    Article  CAS  PubMed  Google Scholar 

  20. Ohkura, H. & Yanagida, M. Cell 64, 149–157 (1991).

    Article  CAS  PubMed  Google Scholar 

  21. Sillekens, P.T.G., Beijer, R.P., Habets, W.J. & Venrooij, W.J. Nucleic Acids Res. 17, 1893–1906 (1989).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  22. Price, S.R., Evans, P.R. & Nagai, K. Nature 394, 645–650 (1998).

    Article  CAS  PubMed  Google Scholar 

  23. Wu, H., Maciejewski, M.W., Benashski, S.E., Mullen, G.P. & King, S.M. J. Biomol. NMR 13, 309–310 (1999).

    Article  CAS  PubMed  Google Scholar 

  24. Bartels, C., Xia, T., Billeter, M., Guntert, P. & Wuthrich, K. J. Biomol. NMR 6, 1–10 (1995).

    Article  CAS  PubMed  Google Scholar 

  25. Guntert, P., Mumenthaler, C. & Wuthrich, K. J. Mol. Biol. 273, 283–298 (1997).

    Article  CAS  PubMed  Google Scholar 

  26. Mumenthaler, C., Guntert, P., Braun, W. & Wuthrich, K. J. Biomol. NMR 10, 351–362 (1997).

    Article  CAS  PubMed  Google Scholar 

  27. Brunger, A.T. X-PLOR: a system for X-ray crystallography and NMR. (Yale University Press, New Haven, Connecticut; 1992).

    Google Scholar 

  28. Koradi, R., Billeter, M. & Wuthrich, K. J. Mol. Graphics 14, 51–55 (1996).

    Article  CAS  Google Scholar 

  29. King, S.M., Otter, T. & Witman, G.B. Methods Enzymol. 134, 291–306 (1986).

    Article  CAS  PubMed  Google Scholar 

  30. Holm, L. & Sander, C. J. Mol. Biol. 233, 123–138 (1993).

    Article  CAS  PubMed  Google Scholar 

  31. Liang, J., Jaffrey, S.R., Snyder, S.H. & Clardy, J. Nature Struct. Biol. 6, 735–740 (1999).

    Article  CAS  PubMed  Google Scholar 

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Acknowledgements

This study was supported by NIH grants to S.M.K. and G.P.M. and by an NIH postdoctoral fellowship to M.W.M.

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Authors and Affiliations

  1. Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, 06032-3305, Connecticut, USA

    Hongwei Wu, Mark W. Maciejewski, Assen Marintchev, Sharon E. Benashski, Gregory P. Mullen & Stephen M. King

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  1. Hongwei Wu
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Correspondence to Gregory P. Mullen or Stephen M. King.

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Wu, H., Maciejewski, M., Marintchev, A. et al. Solution structure of a dynein motor domain associated light chain. Nat Struct Mol Biol 7, 575–579 (2000). https://doi.org/10.1038/76804

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