Abstract
Sodium-transloating ATPase in the fermentative bacteriumStreptococcus faecalis exchanges sodium for potassium ions. Sodium ions stimulate its activity, but K+ ions have no significant effect at present. Although the molecular nature of the sodium ATPase is not clear, the enzyme is distinct from other ion-motive ATPases (E1E2 type and F1F0 type) as judged by its resistance to vanadate as well as dicyclohexylcarbodiimde. The sodium ATPase is induced when cells are grown on media rich in sodium, particularly under conditions that limit the generation of a proton potential or block the constitutive sodium/proton antiporter, indicating that an increase in the cytoplasmic sodium level serves as the signal. The enzyme is not induced in response to K+ deprivation. The sodium ATPase may have evolved to cope with a sodium-rich environment under conditions that limit the magnitude of the proton potential.
Similar content being viewed by others
References
Bakker, E. P., and Harold, F. M. (1980).J. Biol. Chem. 255, 433–440.
Benyoucef, M., Rigaud, J-L., and Leblanc, G. (1982).Biochem. J. 208, 539–547.
Carper, S. W., and Lancaster, J. R. (1986).FEBS Lett. 200, 177–180.
Deibel, R. H., and Seeley, H. W., Jr. (1974).Genus I. Streptococcus, InBergey's Manual of Determinative Bacteriology (Buchanan, R. E., and Gibbons, N. E., eds.), 8th edn., Williams and Wilkins, Baltimore, p. 490.
Dibrov, P. A., Skulachev, V. P., Sokolov, M. V., and Verkhovskaya, M. L. (1988).FEBS Lett. 233, 355–358.
Fürst, P., and Solioz, M. (1986).J. Biol. Chem. 251, 4302–4308.
Harold, F. M. (1986).The Vital Force: A Study of Bioenergetics, Freeman, New York.
Harold, F. M., and Papineau, D. (1972).J. Membr. Biol. 8, 45–62.
Harold, F. M., and Altendorf, K. (1974).Curr. Top. Membr. Transport 5, 1–50.
Harold, F. M., and Kakinuma, Y. (1985).Ann. N.Y. Acad. Sci. 456, 375–383.
Harold, F. M., Baarda, J. R., and Pavlasova, E. (1970).J. Bacteriol. 101, 152–157.
Heefner, D. L. (1982).Mol. Cell. Biochem. 44, 81–106.
Heefner, D. L., and Harold, F. M. (1980).J. Biol. Chem. 255, 11396–11402.
Heefner, D. L., and Harold, F. M. (1982).Proc. Natl. Acad. Sci. USA 79, 2798–2802.
Heefner, D. L., Kobayashi, H., and Harold, F. M. (1980).J. Biol. Chem. 255, 11403–11407.
Jinks, D. C., Silvius, J. R., and McElhaney, R. N. (1978).J. Bacteriol. 136, 1027–1036.
Kakinuma, Y. (1987a).J. Bacteriol. 169, 3886–3890.
Kakinuma, Y. (1987b).J. Bacteriol. 169, 4403–4405.
Kakinuma, Y., and Harold, F. M. (1985).J. Biol. Chem. 260, 2086–2091.
Kakinuma, Y., and Igarashi, K. (1988).J. Biol. Chem. 263, 14166–14170.
Kashket, E. R. (1979).J. Biol. Chem. 254, 8129–8131.
Kashket, E. R., and Barker, S. L. (1977).J. Bacteriol. 130, 1017–1023.
Kinoshita, N., Unemoto, T., and Kobayashi, H. (1984).J. Bacteriol. 158, 844–848.
Kobayashi, H. (1982).J. Bacteriol. 150, 506–511.
Kobayashi, H., and Kakinuma, Y. (1985). Cation Transport ATPase in Bacteria. InProgress in Bioenergetics in Japan. pp. 65–66.
Krulwich, T. A. (1983).Biochim. Biophys. Acta 726, 245–264.
Lanyi, J. K. (1979).Biochim. Biophys. Acta 559, 377–398.
Laubinger, W., and Dimroth, P. (1987).Eur. J. Biochem. 168, 475–480.
Laubinger, W., and Dimroth, P. (1988).Biochemistry 27, 7531–7537.
Lewis, R. N. A. H., and McElhaney, R. N. (1983).Biochem. Biophys. Acta 735, 113–122.
Mitchell, P. (1976).Biochem. Soc. Trans. 4, 399–430.
Russell, J. B., Strobel, H. J., Driessen, A. M., and Konings, W. N. (1988).J. Bacteriol. 170, 3531–3536.
Skulachev, V. P. (1985).Eur. J. Biochem. 151, 199–208.
Skulachev, V. P. (1988).Membrane Bioenergetics, Springer-Verlag, Berlin, Heidelberg.
West, I. C., and Mitchell, P. (1974).Biochem. J. 144, 87–90.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kakinuma, Y., Igarashi, K. Sodium-translocating adenosine triphosphatase inStreptococcus faecalis . J Bioenerg Biomembr 21, 679–692 (1989). https://doi.org/10.1007/BF00762686
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00762686