Biochemical Characterization of the Fungal Plasma Membrane ATPase, An Electrogenic Proton Pump

  • Carolyn W. Slayman


From a variety of flux and electrophysiological studies, it has become clear that there is a rapid and physiologically important circulation of protons across the fungal plasma membrane (Eddy, 1978; Goffeau and Slayman, 1981). Protons are pumped outwards by a primary ATPase, generating both a pH gradient (up to 3 pH units) and a membrane potential (150 to 250 mV, inside negative), and return inwards by way of H+-dependent cotransport systems for sugars, amino acids, and inorganic ions (Fig. 1). A major goal of research during the past few years has been to establish the molecular structure of the fungal plasma membrane ATPase. In particular, there has been reason to ask whether it belongs to the F0F1 class of mitochondrial, chloroplast, and bacterial ATPases (which are capable of ATP-driven proton translocation, even though they usually function in the opposite direction to synthesize ATP), or whether it is more closely related to the Na+/K+-ATPase, Ca2+-ATPase and H+/K+-ATPase of animal cells (which act physiologically in the “transport” direction to pump cations across their respective membranes).


Candida Tropicalis Schizosaccharomyces Pombe Proton Translocation Mitochondrial ATPase Fungal Plasma Membrane 
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  1. Ahlers, J., Ahr, E., and Seyforth, A. (1978). Mol. Cell. Biochem. 22, 39–49.CrossRefGoogle Scholar
  2. Amory, A., Foury, F., and Goffeau, A. (1980). J. Biol. Chem. 255, 9353–9357.Google Scholar
  3. Blasco, F., Chapuis, J. P., and Giordani, R. (1981). Biochimie 63, 507–514.CrossRefGoogle Scholar
  4. Borst-Pauwels, G. W. F. H., and Peeters, P. H. J. (1981). Biochim. Biophys. Acta, 642, 173–186.CrossRefGoogle Scholar
  5. Bowman, B. J., and Slayman, C. W. (1977). J. Biol. Chem. 252, 3357–3363.Google Scholar
  6. Bowman, B. J., and Slayman, C. W. (1979). J. Biol. Chem. 254, 2928–2934.Google Scholar
  7. Bowman, B. J., Blasco, F., and Slayman, C. W. (1978a). In Frontiers of Biological Energetics (P. L. DuttonGoogle Scholar
  8. J. S. Leigh, and A. Scarpa, eds.), Vol. 1, pp. 525–533, Academic Press, New York.Google Scholar
  9. Bowman, B. J., Mainzer, S. E., Allen, K. E., and Slayman, C. W. (1978b). Biochim. Biophys. Acta 512, 13–28.CrossRefGoogle Scholar
  10. Bowman, B. J., Blasco, F., and Slayman, C. W. (1981a), J. Biol. Chem., 256, 12343–12349.Google Scholar
  11. Bowman, E. J., Bowman, B. J., and Slayman, C. W. (1981b). J. Biol. Chem., 256, 12336–12342.Google Scholar
  12. Dame, J. B., and Scarborough, G. A. (1980). Biochemistry 19, 2931–2937.CrossRefGoogle Scholar
  13. Delhez, J. Dufour, J.-P., Thines, D., and Goffeau, A. (1977). Eur. J. Biochem. 79 319–328.Google Scholar
  14. Dufour, J.-P., and Goffeau, A. (1978). J. Biol. Chem. 253, 7026–7032.Google Scholar
  15. Dufour, J.-P, and Goffeau, A. L. (1980). Eur. J. Biochem. 105, 145–154.CrossRefGoogle Scholar
  16. Dufour, J.-P, and Goffeau, A. L. (1981). J. Biol. Chem., 255, 10591–10598.Google Scholar
  17. Dufour, J.-P., and Tsong, T. Y. (1981). J. Biol. Chem., 256, 1801–1808.Google Scholar
  18. Eddy, A. A. (1978). Curr. Top. Membr. Transp. 10, 279–360.CrossRefGoogle Scholar
  19. Fuhrman, G. F., Boehm, C., and Theuvenet, A. P. R. (1976). Biochim. Biophys. Acta 433, 583–596.CrossRefGoogle Scholar
  20. Goffeau, A. L., and Slayman, C. W. (1981). Biochim. Biophys. Acta,in press. Malpartida, F., and Serrano, R. (1980). FEBS Lett. 111 69–72.Google Scholar
  21. Peeters, P. H. J., and Borst-Pauwels, G. W. F. H. (1979). Physiol. Plant. 46, 330–337. Perlin, D. S., and Slayman, C. W. (1981). Fed. Proc. 40, 1784.Google Scholar
  22. Scarborough, G. A. (1975). J. Biol. Chem. 250, 1106–1111.Google Scholar
  23. Scarborough, G. A. (1976). Proc. Natl. Acad. Sci. USA 73, 1485–1488. Scarborough, G. A. (1977). Arch. Biochem. Biophys. 180, 384–393. Scarborough, G. A. (1980). Biochemistry 19, 2925–2931.Google Scholar
  24. Serrano, R. (1978). Mol. Cell. Biochem. 22, 51–62.CrossRefGoogle Scholar
  25. Stroobant, P., and Scarborough, G. A. (1979). Anal. Biochem. 95, 554–558.CrossRefGoogle Scholar
  26. Willsky, G. R. (1979). J. Biol. Chem. 254, 3326–3332.Google Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Carolyn W. Slayman
    • 1
  1. 1.Departments of Human Genetics and PhysiologyYale University School of MedicineNew HavenUSA

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