Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1987 Apr;83(4):994–1000. doi: 10.1104/pp.83.4.994

The Ca2+-Transport ATPase of Plant Plasma Membrane Catalyzes a nH+/Ca2+ Exchange 1

Franca Rasi-Caldogno 1,2, Maria C Pugliarello 1,2, Maria I De Michelis 1,2
PMCID: PMC1056489  PMID: 16665378

Abstract

Microsomal vesicles from 24-hour-old radish (Raphanus sativus L.) seedlings accumulate Ca2+ upon addition of MgATP. MgATP-dependent Ca2+ uptake co-migrates with the plasma membrane H+-ATPase on a sucrose gradient. Ca2+ uptake is insensitive to oligomycin, inhibited by vanadate (IC50 40 micromolar) and erythrosin B (IC50 0.2 micromolar) and displays a pH optimum between pH 6.6 and 6.9. MgATP-dependent Ca2+ uptake is insensitive to protonophores. These results indicate that Ca2+ transport in these microsomal vesicles is catalyzed by a Mg2+-dependent ATPase localized on the plasma membrane. Ca2+ strongly reduces ΔpH generation by the plasma membrane H+-ATPase and increases MgATP-dependent membrane potential difference (Δψ) generation. These effects of Ca2+ on ΔpH and Δψ generation are drastically reduced by micromolar erythrosin B, indicating that they are primarily a consequence of Ca2+ uptake into plasma membrane vesicles. The Ca2+-induced increase of Δψ is collapsed by permeant anions, which do not affect Ca2+-induced decrease of ΔpH generation by the plasma membrane H+-ATPase. The rate of decay of MgATP-dependent ΔpH, upon inhibition of the plasma membrane H+-ATPase, is accelerated by MgATP-dependent Ca2+ uptake, indicating that the decrease of ΔpH generation induced by Ca2+ reflects the efflux of H+ coupled to Ca2+ uptake into plasma membrane vesicles. It is therefore proposed that Ca2+ transport at the plasma membrane is mediated by a Mg2+-dependent ATPase which catalyzes a nH+/Ca2+ exchange.

Full text

PDF
998

Selected References

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

  1. Blumwald E., Poole R. J. Kinetics of Ca/H Antiport in Isolated Tonoplast Vesicles from Storage Tissue of Beta vulgaris L. Plant Physiol. 1986 Mar;80(3):727–731. doi: 10.1104/pp.80.3.727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bush D. R., Sze H. Calcium transport in tonoplast and endoplasmic reticulum vesicles isolated from cultured carrot cells. Plant Physiol. 1986 Feb;80(2):549–555. doi: 10.1104/pp.80.2.549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chiesi M., Inesi G. Adenosine 5'-triphosphate dependent fluxes of manganese and and hydrogen ions in sarcoplasmic reticulum vesicles. Biochemistry. 1980 Jun 24;19(13):2912–2918. doi: 10.1021/bi00554a015. [DOI] [PubMed] [Google Scholar]
  4. Dieter P., Marmé D. Calmodulin activation of plant microsomal Ca uptake. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7311–7314. doi: 10.1073/pnas.77.12.7311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hodges T. K., Hanson J. B. Calcium Accumulation by Maize Mitochondria. Plant Physiol. 1965 Jan;40(1):101–109. doi: 10.1104/pp.40.1.101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kimber A., Sze H. Helminthosporium maydis T Toxin Decreased Calcium Transport into Mitochondria of Susceptible Corn. Plant Physiol. 1984 Apr;74(4):804–809. doi: 10.1104/pp.74.4.804. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lew R. R., Briskin D. P., Wyse R. E. Ca uptake by endoplasmic reticulum from zucchini hypocotyls : the use of chlorotetracycline as a probe for ca uptake. Plant Physiol. 1986 Sep;82(1):47–53. doi: 10.1104/pp.82.1.47. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Meissner G. Calcium transport and monovalent cation and proton fluxes in sarcoplasmic reticulum vesicles. J Biol Chem. 1981 Jan 25;256(2):636–643. [PubMed] [Google Scholar]
  9. Morris S. J., Silbergeld E. K., Brown R. R., Haynes D. H. Erythrosin B (USFD&C RED 3) inhibits calcium transport and atpase activity of muscle sarcoplasmic reticulum. Biochem Biophys Res Commun. 1982 Feb 26;104(4):1306–1311. doi: 10.1016/0006-291x(82)91392-4. [DOI] [PubMed] [Google Scholar]
  10. Niggli V., Sigel E., Carafoli E. The purified Ca2+ pump of human erythrocyte membranes catalyzes an electroneutral Ca2+-H+ exchange in reconstituted liposomal systems. J Biol Chem. 1982 Mar 10;257(5):2350–2356. [PubMed] [Google Scholar]
  11. Ohsumi Y., Anraku Y. Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J Biol Chem. 1983 May 10;258(9):5614–5617. [PubMed] [Google Scholar]
  12. Okorokov L. A., Kulakovskaya T. V., Lichko L. P., Polorotova E. V. H+/ion antiport as the principal mechanism of transport systems in the vacuolar membrane of the yeast Saccharomyces carlsbergensis. FEBS Lett. 1985 Nov 18;192(2):303–306. doi: 10.1016/0014-5793(85)80130-7. [DOI] [PubMed] [Google Scholar]
  13. Rasi-Caldogno F., De Michelis M. I., Pugliarello M. C., Marrè E. H-pumping driven by the plasma membrane ATPase in membrane vesicles from radish: stimulation by fusicoccin. Plant Physiol. 1986 Sep;82(1):121–125. doi: 10.1104/pp.82.1.121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Rasi-Caldogno F., Pugliarello M. C., De Michelis M. I. Electrogenic transport of protons driven by the plasma membrane ATPase in membrane vesicles from radish : biochemical characterization. Plant Physiol. 1985 Jan;77(1):200–205. doi: 10.1104/pp.77.1.200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Roufogalis B. D., Akyempon C. K., Al-Jobore A., Minocherhomjee A. M. Regulation of the Ca2+ pump of the erythrocyte membrane. Ann N Y Acad Sci. 1982;402:349–367. doi: 10.1111/j.1749-6632.1982.tb25754.x. [DOI] [PubMed] [Google Scholar]
  16. Schumaker K. S., Sze H. A Ca/H Antiport System Driven by the Proton Electrochemical Gradient of a Tonoplast H-ATPase from Oat Roots. Plant Physiol. 1985 Dec;79(4):1111–1117. doi: 10.1104/pp.79.4.1111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Stroobant P., Scarborough G. A. Active transport of calcium in Neurospora plasma membrane vesicles. Proc Natl Acad Sci U S A. 1979 Jul;76(7):3102–3106. doi: 10.1073/pnas.76.7.3102. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES