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Journal of Bioenergetics and Biomembranes

, Volume 25, Issue 6, pp 671–678 | Cite as

Evidence for three different electrophoretic pathways in yeast mitochondria: Ion specificity and inhibitor sensitivity

  • Stéphen Manon
  • Martine Guérin
Original Articles

Abstract

We identified three electrophoretic pathways by spectrophotometrically following the swelling of isolated yeast mitochondria:
  • --An anion uniport whose activity could only be detected after depletion of divalent cations from the matrix by treatment with 1,10-phenanthroline. This uniport was inhibited by Mg2+ and dicyclohexylcarbodiimide.

  • --A K+(Na+) uniport which was detected only when mitochondria were suspended at low pH and low temperature. This uniport was sensitive to ruthenium red and oleic acid.

  • --A K+ selective uniport which was activated by alkaline pH and ATP depletion. This pathway was sensitive to glibenclamide and to various amphiphilic cations.

Similarities and differences between these three electrophoretic pathways and the electrophoretic systems described in mammalian and plant mitochondria are discussed.

Key words

Transport mitochondria ion translocation 

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References

  1. Antonenko, Y. N., Kinnally, K. W., and Tedeshi, H. (1991).J. Membr. Biol. 124, 15–158.Google Scholar
  2. Arselin de Châteaubodeau, G., Guérin, M., and Guérin, B. (1976).Biochimie (Paris) 58, 601–610.Google Scholar
  3. Beauvoit, B., Rigoulet, M., and Guérin, B. (1989).FEBS Lett. 244, 255–258.Google Scholar
  4. Beavis, A. D. (1992).J. Bioenerg. Biomembr 24, 77–90.Google Scholar
  5. Beavis, A. D., and Garlid, K. D. (1987).J. Biol. Chem. 262, 15085–15093.Google Scholar
  6. Beavis, A. D., and Vercesi, A. E. (1992).J. Biol. Chem. 267, 3079–3087.Google Scholar
  7. Beavis, A. D., Lu, Y., and Garlid, K. D. (1993).J. Biol. Chem. 268, 997–1004.Google Scholar
  8. Bernardi, P., Angrilli, A., Azzone, G. F. (1990).Eur. J. Biochem. 188, 91–97.Google Scholar
  9. Bernardi, P., Vassanelli, S., Veronese, P., Colonna, R., Szabo, I., and Zoratti, M. (1992).J. Biol. Chem. 267, 2934–2939.Google Scholar
  10. Bernardi, P., Veronese, P., and Petronilli, V. (1993).J. Biol. Chem. 268, 1005–1010.Google Scholar
  11. Bradford, M. M. (1976).Anal. Biochem. 72, 248–254.Google Scholar
  12. Carafoli, E., Balcavage, W. X., Lehninger, A. L., and Mattoon, J. R. (1970).Biochim. Biophys. Acta 205, 18–20.Google Scholar
  13. Costa, G., Kinnally, K. W., and Diwan, J. J. (1991).Biochem. Biophys. Res. Commun. 175, 305–310.Google Scholar
  14. Dabadie, P., Jean-Bart, E., Mazat, J. P., and Guérin, B. (1986) 4th E.B.E.C. reports, p. 288.Google Scholar
  15. Davis, N. W., Standen, N. B., and Stanfield, P. R. (1991).J. Bioenerg. Biomembr. 23, 509–535.Google Scholar
  16. Diwan, J. J., Haley, T., and Sanadi, D. R. (1988).Biochem. Biophys. Res. Commun. 153, 224–230.Google Scholar
  17. Garlid, K. D., Shariat-Madar, Z., Nath, S., and Jezek, P. (1991).J. Biol. Chem. 266, 6518–6523.Google Scholar
  18. Guérin, B., Labbe, P., and Somlo, M. (1977).Methods Enzymol. 55, 149–159.Google Scholar
  19. Gunter, T. E., and Pfeiffer, D. R. (1990).Am. J. Physiol. 258, C755-C786.Google Scholar
  20. Hanson, J. B. (1985). InEncyclopedia of Plant Physiology (Douce, R., and Day, D. A., eds.), Vol. 18, Springer-Verlag, Berlin, pp. 248–280.Google Scholar
  21. Higuti, T., Arakaki, N., Niimi, S., Nakasima, S., Saito, R., Tani, L., and Ota, F. (1980).J. Biol. Chem. 255, 7631–7636.Google Scholar
  22. Inoue, I., Nagase, H., Kishi, K., and Higuti, T. (1991).Nature (London) 352, 244–247.Google Scholar
  23. Jung, D. W., Chàvez, E., and Brierley, G. P. (1977).Arch. Biochem. Biophys. 183, 452–459.Google Scholar
  24. Kapus, A., Szaszi, A., Kaldi, K., Ligeti, E., and Fonyo, A. (1990).J. Biol. Chem. 265, 18063–18066.Google Scholar
  25. Kapus, A., Szaszi, A., Kaldi, K., Ligeti, E., and Fonyo, A. (1991).FEBS Lett. 282, 61–64.Google Scholar
  26. Kinnally, K. W., Campo, M. L., and Tedeshi, H. (1989).J. Bioenerg. Biomembr. 21, 497–506.Google Scholar
  27. Kinnally, K. W., Zorov, D. B., Antonenko, Y. M., and Perini, S. (1991).Biochem. Biophys. Res. Commun. 176, 1183–1189.Google Scholar
  28. Kinnally, K. W., Antonenko, Y. N., and Zorov, D. B. (1992).J. Bioenerg. Biomembr. 24, 99–110.Google Scholar
  29. Li, X., Hegazy, M. G., Mahdi, F., Jezek, P., Lane, R. D., and Garlid, K. D. (1990).J. Biol. Chem. 265, 15316–15322.Google Scholar
  30. Li, W., Shariat-Madar, Z., Powers, M., Sun, X., Lane, R. D., and Garlid, K. D. (1992).J. Biol. Chem. 267, 17983–17989.Google Scholar
  31. Manon, S., and Guérin, M. (1992).Biochim. Biophys. Acta 1108, 169–176.Google Scholar
  32. Manon, S., and Guérin, M. (1993).Biochem. Mol. Biol. Int. 29, 375–385.Google Scholar
  33. Mitchell, P. (1966).Biol. Rev. 41, 445–502.Google Scholar
  34. Moran, O., Sciancalepore, M., Sandri, G., Panfili, E., Bassi, R., Ballarin, C., and Sorgato, M. C. (1992).Eur. Biophys. J. 20, 311–319.Google Scholar
  35. Nakashima, R. A., and Garlid, K. D. (1982).J. Biol. Chem. 257, 9252–9254.Google Scholar
  36. Nicolli, A., Redetti, A., and Bernardi, P. (1991).J. Biol. Chem. 266, 9465–9470.Google Scholar
  37. Novgorodov, S. A., Gudz, T. I., Milgrom, Y. M., and Brierley, G. P. (1992).J. Biol. Chem. 267, 16274–16282.Google Scholar
  38. Paliwal, R., Costa, G., and Diwan, J. J. (1992).Biochemistry 31, 2223–2229.Google Scholar
  39. Paucek, P., Mironova, G., Mahdi, F., Beavis, A., Woldegiorgis, G., and Garlid, K. D. (1992).J. Biol. Chem. 267, 26062–26069.Google Scholar
  40. Petronilli, V., Szabo, I., and Zoratti, M. (1989).FEBS Lett. 259, 137–143.Google Scholar
  41. Powers, M. F., and Beavis, A. D. (1991).J. Biol. Chem. 266, 17250–17256.Google Scholar
  42. Sorgato, M. C., and Moran, O. (1993).Crit. Rev. Biochem. Mol. Biol. 18, 127–171.Google Scholar
  43. Sorgato, M. C., Keller, B. U., and Stuhmer W. (1987).Nature (London) 330, 498–500.Google Scholar
  44. Szabo, I., and Zoratti, M. (1991).J. Biol. Chem. 266, 3376–3379.Google Scholar
  45. Velours, J., Rigoulet, M., and Guérin, B. (1977).FEBS Lett. 81, 18–22.Google Scholar

Copyright information

© Plenum Publishing Corporation 1993

Authors and Affiliations

  • Stéphen Manon
    • 1
  • Martine Guérin
    • 1
  1. 1.Institut de Biochimie Cellulaire du CNRSUniversité de Bordeaux IIBordeauxFrance

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