Genetics of the Adenosine Triphosphatase Complex of Escherichia coli

  • J. Allan Downie
  • Frank Gibson
  • Graeme B. Cox

Abstract

The ATPase complex from Escherichia coli, like that from many sources, can be dissociated into two portions known as the F1-ATPase, which contains the catalytic site for ATP hydrolysis, and the F0 portion, which is located within the membrane and appears to act as a proton channel (Fillingame, 1980).

Keywords

Hydrolysis Urea Adenosine Polypeptide Succinate 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bragg, P. D., and Hou, C. (1975). Arch. Biochem. Biophys. 167, 311–321.CrossRefGoogle Scholar
  2. Bragg, P. D., and Hou, C. (1980). Biochem. Biophys. Res. Commun. 95, 952–957.CrossRefGoogle Scholar
  3. Butlin, J. D., Cox, G. B., and Gibson, F. (1971). Biochem. J. 124, 75–81.Google Scholar
  4. Butlin, J. D., Cox, G. B., and Gibson, F. (1973). Biochim. Biophys. Acta 292, 366–375.CrossRefGoogle Scholar
  5. Cox, G. B., Gibson, F., and McCann, L. (1973). Biochem. J. 134, 1015–1021.Google Scholar
  6. Downie, J. A., Gibson, F., and Cox, G. B. (1979). Annu. Rev. Biochem. 48, 103–131.CrossRefGoogle Scholar
  7. Downie, J. A., Langman, L., Cox, G. B., Yanofsky, C., and Gibson, F. (1980). J. Bacteriol. 143, 8–17.Google Scholar
  8. Downie, J. A., Cox, G. B., Langman, L., Ash, G., Becker, M., and Gibson, F. (1981). J. Bacteriol. 145, 200–210.Google Scholar
  9. Dunn, S. D. (1978). Biochem. Biophys. Res. Commun. 82, 596–602.CrossRefGoogle Scholar
  10. Fayle, D. R. H., Downie, J. A., Cox, G. B., Gibson, F., and Radik, J. (1978). Biochem. J. 172, 523–531.Google Scholar
  11. Fillingame, R. H. (1980). Annu. Rev. Biochem. 49, 1079–1113.CrossRefGoogle Scholar
  12. Foster, D. L., and Fillingame, R. H. (1979). J. Biol. Chem. 254, 8230–8236.Google Scholar
  13. Friedl, P., Friedl, C., and Schairer, H. U. (1979). Eur. J. Biochem. 100, 175–180.CrossRefGoogle Scholar
  14. Gay, N. J., and Walker, J. E. (1981). Nucleic Acids Research 9, 3919–3926.CrossRefGoogle Scholar
  15. Gibson, F., Cox, G. B., Downie, J. A., and Radik, J. (1977). Biochem. J. 164, 193–198.Google Scholar
  16. Gibson, F., Downie, J. A., Cox, G. B., and Radik, J. (1978). J. Bacteriol. 134, 728–736.Google Scholar
  17. Gutnick, D. L., Kanner, B. I., and Postma, P. W. (1972). Biochim. Biophys. Acta 283, 217–222.CrossRefGoogle Scholar
  18. Kanazawa, H., Saito, S., and Futai, M. (1978). J. Biochem. 84, 1513–1517.Google Scholar
  19. Kanazawa, H., Horiuchi, Y., Takagi, M., Ishino, Y., and Futai, M. (1980). J. Biochem. 88, 695–703.Google Scholar
  20. Kanazawa, H., Mabuchi, K., Kayano, T., Noumi, T., Sekiya, T., and Futai, M. (1981). Biochem. Biophys. Res. Commun. 103, 613–620.CrossRefGoogle Scholar
  21. Negrin, R. S., Foster, D. L., and Fillingame, R. H. (1980). J. Biol. Chem. 255, 5643–5648.Google Scholar
  22. Rosen, B. P., and Hasan, S. M. (1979). FEBS Lett. 104, 339–342.CrossRefGoogle Scholar
  23. Schneider, E., and Altendorf, K. (1980). FEBS Lett. 116, 173–176.CrossRefGoogle Scholar
  24. Senior, A. E., Downie, J. A., Cox, G. B., Gibson, F., Langman, L., and Fayle, D. R. H. (1979a). Biochem. J. 180, 103–109.Google Scholar
  25. Senior, A. E., Fayle, D. R. H., Downie, J. A., Gibson, F., and Cox, G. B. (1979b). Biochem. J. 180, 110–118.Google Scholar
  26. Verheijen, J. H., Postma, P. W., and Van Dam, K. (1980). FEBS Lett. 116, 307–309.CrossRefGoogle Scholar
  27. Vogel, G., and Steinhart, R. (1976). Biochemistry 15, 208–216.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • J. Allan Downie
    • 1
  • Frank Gibson
    • 1
  • Graeme B. Cox
    • 1
  1. 1.Biochemistry Department, John Curtin School of Medical ResearchAustralian National UniversityCanberraAustralia

Personalised recommendations