Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins

Abstract

The ABC excision nuclease of Escherichia coll is an ATP-depen-dent DNA repair enzyme composed of three protein subunits, UvrA, UvrB and UvrC. The DNA sequences of all three genes have been reported1–3. UvrA, the component that binds directly to the DNA, and UvrB, which attaches itself to the UvrA-DNA complex, both contain consensus sequences thought to be diagnostic of ATP-binding sites4, although the UvrC sequence does not. We now report that a computer analysis of the UvrA sequence has revealed an unusual series of internal duplications centering around putative metal-binding sites which may be involved in the interaction with DNA. We also find a strong evolutionary relationship to a family of prokaryotic membrane-associated active-transport proteins.

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

Access options

Buy this article

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

Similar content being viewed by others

References

  1. Husain, I., Van Houten, B., Thomas, D. C. & Sancar, A. J. biol. Chem. 261, 4895–4901 (1986).

    CAS  PubMed  Google Scholar 

  2. Arikan, E., Kulkarni, M. S., Thomas, D. C. & Sancar, A. Nucleic Acids Res. 14, 2637–2650 (1986).

    Article  CAS  Google Scholar 

  3. Sancar, G. B., Sancar, A. & Rupp, W. D. Nucleic Acids Res. 12, 4593–4608 (1984).

    Article  CAS  Google Scholar 

  4. Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. EMBO J. 1, 945–951 (1982).

    Article  CAS  Google Scholar 

  5. Miller, J., McLachlan, A. D. & Klug, A. EMBO J. 4, 1609–1614 (1985).

    Article  CAS  Google Scholar 

  6. Berg, J. M. Science 232, 485–487 (1986).

    Article  ADS  CAS  Google Scholar 

  7. Hobson, A. C., Weatherwax, R. & Ferro-Luzzi Ames, G. Proc. natn. Acad. Sci. U.S.A. 81, 7333–7337 (1984).

    Article  ADS  CAS  Google Scholar 

  8. Gilson, E., Higgins, C. F., Hofnung, M., Ferro-Luzzi Ames, G. & Nikaido, H. J. biol. Chem. 257, 9915–9918 (1982).

    CAS  PubMed  Google Scholar 

  9. Higgins, C. F., Hiles, I. D., Whalley, K. & Jamieson, D.J. EMBO J. 4, 1033–1040 (1985).

    Article  CAS  Google Scholar 

  10. Surin, B. P., Rosenberg, H. & Cox, G. J. Bact. 161, 189–198 (1985).

    CAS  PubMed  Google Scholar 

  11. Feng, D.-F., Johnson, M. S. & Doolittle, R. F. J. molec. Evol. 21, 112–125 (1985).

    Article  ADS  CAS  Google Scholar 

  12. Doolittle, R. F. in Protein Engineering(ed. Inouye, M.) (Academic, New York, in the press).

  13. Gilson, E., Nikaido, H. & Hofnung, M. Nucleic Acids Res. 10, 7449–7458 (1982).

    Article  CAS  Google Scholar 

  14. Dunn, J. J. & Studier, F. W. J. J. molec. Biol. 148,303–330 (1981).

    Article  CAS  Google Scholar 

  15. Burton, Z. F., Gross, C. A., Watanabe, K. K. & Burgess, R. R. Cell 32, 335–349 (1983).

    Article  CAS  Google Scholar 

  16. Ferro-Luzzi Ames, G. Curr. Topics Membrane Transport 23, 103–119 (1985).

    Article  Google Scholar 

  17. Sancar, A. & Rupp, W. D. Cell 33, 249–260 (1983).

    Article  CAS  Google Scholar 

  18. Van Duin, M. et al. cell 44, 913–923 (1986).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Doolittle, R., Johnson, M., Husain, I. et al. Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins. Nature 323, 451–453 (1986). https://doi.org/10.1038/323451a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/323451a0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing