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. 1985 Jul 15;229(2):459–467. doi: 10.1042/bj2290459

The control by delta mu H+ of the tonoplast-bound H+-translocating adenosine triphosphatase from rubber-tree (Hevea brasiliensis) latex.

B P Marin
PMCID: PMC1145078  PMID: 2994636

Abstract

The relationship between tonoplast-bound ATPase activity and the magnitude of the electrochemical proton gradient has been investigated on tightly sealed vesicles prepared from rubber-tree (Hevea brasiliensis) latex. A variety of methods have been used to modify, either alone or together, the two components of the electrochemical proton gradient (delta mu H+). When the delta pH component was decreased either by titration with (NH4)2SO4 or by addition of protonophores or nigericin in the presence of K+, ATPase activity was stimulated. On the other hand, when the delta psi component was decreased either by addition of lipophilic cations or by addition of valinomycin in the presence of K+, ATPase activity decreased. It is concluded that activity of the tonoplast-bound ATPase is regulated by changes in the electrochemical proton gradient across the tonoplast, so that, once the maximum proton gradient is established across the tonoplast, any perturbation of the equilibrium state should result in the increased rate of ATP hydrolysis as the enzyme attempts to re-establish the initial gradient.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amzel L. M., Pedersen P. L. Proton atpases: structure and mechanism. Annu Rev Biochem. 1983;52:801–824. doi: 10.1146/annurev.bi.52.070183.004101. [DOI] [PubMed] [Google Scholar]
  2. Bowman E. J. Comparison of the vacuolar membrane ATPase of Neurospora crassa with the mitochondrial and plasma membrane ATPases. J Biol Chem. 1983 Dec 25;258(24):15238–15244. [PubMed] [Google Scholar]
  3. Gould J. M. Inhibition by triphenyltin chloride of a tightly-bound membrane component involved in photophosphorylation. Eur J Biochem. 1976 Mar 1;62(3):567–575. doi: 10.1111/j.1432-1033.1976.tb10191.x. [DOI] [PubMed] [Google Scholar]
  4. Heinonen J. K., Lahti R. J. A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal Biochem. 1981 May 15;113(2):313–317. doi: 10.1016/0003-2697(81)90082-8. [DOI] [PubMed] [Google Scholar]
  5. Johnson R. G., Beers M. F., Scarpa A. H+ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry. J Biol Chem. 1982 Sep 25;257(18):10701–10707. [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Maloney P. C. Energy coupling to ATP synthesis by the proton-translocating ATPase. J Membr Biol. 1982;67(1):1–12. doi: 10.1007/BF01868643. [DOI] [PubMed] [Google Scholar]
  8. Marin B. P., Gidrol X. Chloride-ion stimulation of the tonoplast H+-translocating ATPase from Hevea brasiliensis (rubber tree) latex. A dual mechanism. Biochem J. 1985 Feb 15;226(1):85–94. doi: 10.1042/bj2260085. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Marin B., Marin-Lanza M., Komor E. The protonmotive potential difference across the vacuo-lysosomal membrane of Hevea brasiliensis (rubber tree) and its modification by a membrane-bound adenosine triphosphatase. Biochem J. 1981 Aug 15;198(2):365–372. doi: 10.1042/bj1980365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Marin B. Sensitivity of tonoplast-bound adenosine-triphosphatase from hevea to inhibitors. Plant Physiol. 1983 Dec;73(4):973–977. doi: 10.1104/pp.73.4.973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ohsumi Y., Anraku Y. Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J Biol Chem. 1981 Mar 10;256(5):2079–2082. [PubMed] [Google Scholar]
  12. Okorokov L. A., Lichko L. P. The identification of a proton pump on vacuoles of the yeast Saccharomyces carlsbergensis. ATPase is electrogenic H+-translocase. FEBS Lett. 1983 May 2;155(1):102–106. doi: 10.1016/0014-5793(83)80218-x. [DOI] [PubMed] [Google Scholar]
  13. Pressman B. C. Biological applications of ionophores. Annu Rev Biochem. 1976;45:501–530. doi: 10.1146/annurev.bi.45.070176.002441. [DOI] [PubMed] [Google Scholar]
  14. Reed P. W. Ionophores. Methods Enzymol. 1979;55:435–454. doi: 10.1016/0076-6879(79)55058-7. [DOI] [PubMed] [Google Scholar]
  15. TAUSSKY H. H., SHORR E. A microcolorimetric method for the determination of inorganic phosphorus. J Biol Chem. 1953 Jun;202(2):675–685. [PubMed] [Google Scholar]
  16. Thom M., Komor E. Role of the ATPase of sugar-cane vacuoles in energization of the tonoplast. Eur J Biochem. 1984 Jan 2;138(1):93–99. doi: 10.1111/j.1432-1033.1984.tb07886.x. [DOI] [PubMed] [Google Scholar]

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