Skip to main content
Log in

Structural evidence for gene duplication in the evolution of the acid proteases

  • Article
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

X-ray studies of acid proteases indicate a bilobal structure with a well defined active site cleft. An intramolecular two-fold symmetry axis relates two topologically similar domains and the active site residues. A possible mechanism for evolution by gene duplication, divergence and gene fusion is presented.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Levitt, M. & Chothia, C. Nature 261, 552–555 (1976).

    Article  ADS  CAS  PubMed  Google Scholar 

  2. Ohlsson, B. et al. J. molec. Biol. 89, 339–354 (1974).

    Article  CAS  PubMed  Google Scholar 

  3. Rossmann, M. G. et al. Nature 250, 194–199 (1974).

    Article  ADS  CAS  PubMed  Google Scholar 

  4. Tang, J. Acid Proteases, Structure–Function and Biology (Plenum, New York, 1977).

    Book  Google Scholar 

  5. Hsu, I-N. et al. in Acid Proteases, Structure–Function and Biology (ed. Tang, J.), 61 (Plenum, New York, 1977).

    Book  Google Scholar 

  6. Hsu, I-N. et al. Nature 266, 140–145 (1977).

    Article  ADS  CAS  PubMed  Google Scholar 

  7. Subramanian, E. et al. Proc. natn. Acad. Sci. U.S.A. 74, 556–559 (1977).

    Article  ADS  CAS  Google Scholar 

  8. Jenkins, J. A. et al. in Acid Proteases, Structure–Function and Biology (ed. Tang, J.) 43 (Plenum, New York, 1977).

    Book  Google Scholar 

  9. Fruton, J. S. Adv. Enzym. 44, 1–36 (1976).

    CAS  Google Scholar 

  10. Tang, J. et al. Proc. natn. Acad. Sci. U.S.A. 70, 3437–3439 (1973).

    Article  ADS  CAS  Google Scholar 

  11. Foltmann, B. & Pedersen, V. B. in Acid Proteases, Structure–Function and Biology (ed. Tang, J.) 3 (Plenum, New York, 1977).

    Book  Google Scholar 

  12. Rossmann, M. G. & Argos, P. J. molec. Biol. 105, 75–96 (1976).

    Article  CAS  PubMed  Google Scholar 

  13. Rossmann, M. G. & Argos, P. J. molec. Biol. 109, 99–129 (1977).

    Article  CAS  PubMed  Google Scholar 

  14. Sepulveda et al. J. biol. Chem. 250, 5082–5088 (1975).

    CAS  PubMed  Google Scholar 

  15. Shotton, D. M. & Watson, H. C. Nature 225, 811–816 (1970).

    Article  ADS  CAS  PubMed  Google Scholar 

  16. Delbaere, L. T. J. et al. Nature 257, 758–763 (1975).

    Article  ADS  CAS  PubMed  Google Scholar 

  17. James, M. N. G. Proc. Miami Winter Symp. 11, 125–142 (1976).

    CAS  Google Scholar 

  18. Altosaar, J. M. et al. Abstracts of IUB Tenth Congress 04-I-L-005 (1976).

  19. Blundell, T. L. et al. Nature 231, 506–511 (1971).

    Article  ADS  CAS  PubMed  Google Scholar 

  20. Eklund, H. et al. J. molec. Biol. 102, 27–59 (1976).

    Article  CAS  PubMed  Google Scholar 

  21. Hardman, K. D. & Ainsworth, C. F. Biochemistry 11, 4910–4918 (1972).

    Article  CAS  PubMed  Google Scholar 

  22. Edelman, G. M. et al. Proc. natn. Acad. Sci. U.S.A. 69, 2580–2585 (1972).

    Article  ADS  CAS  Google Scholar 

  23. Blake, C. C. F. et al. J. molec. Biol. 88, 1–12 (1974).

    Article  CAS  PubMed  Google Scholar 

  24. James, M. N. G. et al. Nature 267, 808–813 (1977).

    Article  ADS  CAS  PubMed  Google Scholar 

  25. Rajagopalan, T. G. et al. J. biol. Chem. 241, 4940–4950 (1966).

    CAS  PubMed  Google Scholar 

  26. Adman, E. T., Sieker, L. C. & Jensen, L. H. J. biol. Chem. 248, 3987–3996 (1973).

    CAS  PubMed  Google Scholar 

  27. Ploegman, J. H., thesis, Univ. Gröningen (1977).

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Tang, J., James, M., Hsu, I. et al. Structural evidence for gene duplication in the evolution of the acid proteases. Nature 271, 618–621 (1978). https://doi.org/10.1038/271618a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/271618a0

  • Springer Nature Limited

This article is cited by

Navigation