Four ATP-binding sites in the midregion of the β heavy chain of dynein (original) (raw)

Nature volume 352, pages 643–645 (1991)Cite this article

Abstract

THE 'motor' proteins of eukaryotic cells contain specialized domains that hydrolyse ATP to produce force and movement along a cytoskeletal polymer (actin in the case of the myosin family; microtubules in the case of the kinesin family and dyneins). There are motor-protein superfamilies in which each member has a conserved force-generating domain joined to a different 'tail' which conveys specific attachment properties (see ref. 1 for a review). The minus-end-directed microtubule motors, the dyneins2, may also constitute a superfamily of force-generating proteins with distinct attachment domains3. Axonemal outer-arm dynein from sea urchin spermatozoa is a multimeric protein consisting of two heavy chains (α and β) with ATPase activity, three intermediate chains and several light chains4. Here I report the sequence of cloned complementary DNA encoding the β heavy chain of a dynein motor molecule. The predicted amino-acid sequence reveals four ATP-binding consensus sequences in the central domain. The dynein β heavy chain is thought to associate transiently with a microtubule during ATP hydrolysis5, but the ATP-dependent microtubule-binding sequence common to the kinesin superfamily is not found in the dynein β heavy chain. These unique features distinguish the dynein β heavy chain from other motor protein superfamilies and may be characteristic of the dynein superfamily.

This is a preview of subscription content, access via your institution

Access options

Subscribe to this journal

Receive 51 print issues and online access

$199.00 per year

only $3.90 per issue

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Additional access options:

Similar content being viewed by others

References

  1. Vale, R. D. & Goldstein, L. S. B. Cell 60, 883–885 (1990).
    Article CAS Google Scholar
  2. Gibbons, I. R. J. Cell Biol. 91, 107s–124s (1981).
    Article CAS Google Scholar
  3. Ogawa, K. et al. Eur. J. Cell Biol. 43, 3–9 (1987).
    CAS PubMed Google Scholar
  4. Tang, W.-J. Y. et al. J. biol. Chem. 257, 508–515 (1982).
    CAS Google Scholar
  5. Sale, W. S. & Fox, L. A. J. Cell Biol. 107, 1793–1797 (1988).
    Article CAS Google Scholar
  6. Ogawa, K. et al. Cell Motil. Cytoskel. 16, 58–67 (1990).
    Article CAS Google Scholar
  7. Nishikawa, K. & Noguchi, T. Meth. Enzym. 202, 31–44 (1991).
    Article CAS Google Scholar
  8. Nishikawa, K. & Ooi, T. J. Biochem. 100, 1043–1046 (1986).
    Article CAS Google Scholar
  9. Ogawa, K. & Mohri, H. J. biol. Chem. 250, 6476–6483 (1975).
    CAS PubMed Google Scholar
  10. Ow, R. A. et al. J. biol. Chem. 262, 3409–3414 (1987).
    CAS PubMed Google Scholar
  11. Ogawa, K. Proc. Japan Acad. 67B, 27–31 (1991).
    Article Google Scholar
  12. Sale, W. S. et al. J. Cell Biol. 101, 1400–1412 (1985).
    Article CAS Google Scholar
  13. Walker, J. E. et al. EMB0 J. 1, 945–951 (1982).
    Article CAS Google Scholar
  14. Gibbons, I. R. et al. J. biol. Chem. 262, 2780–2786 (1987).
    CAS PubMed Google Scholar
  15. Tang, W.-J. Y. & Gibbons, I. R. J. biol. Chem. 262, 17728–17734 (1987).
    CAS PubMed Google Scholar
  16. Pfister, K. K. et al. J. biol. Chem. 259, 8499–8504 (1984).
    CAS PubMed Google Scholar
  17. Lewis, S. L. et al. Science 242, 936–939 (1988).
    Article ADS CAS Google Scholar
  18. Lee, G. et al. Science 239, 285–288 (1988).
    Article ADS CAS Google Scholar
  19. Yang, J. T. et al. Cell 56, 879–889 (1989).
    Article CAS Google Scholar
  20. Kozak, M. Cell 44, 283–292 (1986).
    Article CAS Google Scholar
  21. Matsudaira, P. J. biol. Chem. 262, 10035–10038 (1987).
    CAS PubMed Google Scholar

Download references

Author information

Authors and Affiliations

  1. Department of Cell Biology, National Institute for Basic Biology, Okazaki, 444, Japan
    Kazuo Ogawa

Authors

  1. Kazuo Ogawa
    You can also search for this author inPubMed Google Scholar

Rights and permissions

About this article

Cite this article

Ogawa, K. Four ATP-binding sites in the midregion of the β heavy chain of dynein.Nature 352, 643–645 (1991). https://doi.org/10.1038/352643a0

Download citation