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Volumn 12, Issue 13, 1996, Pages 1301-1313

Evidence for a selective and electroneutral K+/H+-exchange in Saccharomyces cerevisiae using plasma membrane vesicles

Author keywords

K+ H+ exchange; Plasma membrane purification; Saccharomyces cerevisiae; Vesicles reconstitution

Indexed keywords

POTASSIUM;

EID: 0029845496     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0061(199610)12:13<1301::AID-YEA18>3.0.CO;2-A     Document Type: Article
Times cited : (22)

References (37)
  • 1
    • 0021688151 scopus 로고
    • Effects of different salts on the plasma membrane ATPase and on proton transport in yeast
    • Ahlers, J. (1984). Effects of different salts on the plasma membrane ATPase and on proton transport in yeast. Can. J. Biochem. Cell. Biol. 62, 998-1005.
    • (1984) Can. J. Biochem. Cell. Biol. , vol.62 , pp. 998-1005
    • Ahlers, J.1
  • 3
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames, B. N. (1966). Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol. 8, 115-118.
    • (1966) Methods Enzymol. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 4
    • 0023657856 scopus 로고
    • Oxonol VI as an optical indicator for membrane potentials in lipid vesicles
    • Apell, H. J. and Bersch, B. (1987). Oxonol VI as an optical indicator for membrane potentials in lipid vesicles. Biochim. Biophys. Acta 903, 480-494.
    • (1987) Biochim. Biophys. Acta , vol.903 , pp. 480-494
    • Apell, H.J.1    Bersch, B.2
  • 5
    • 0027415536 scopus 로고
    • + channel from the plasma membrane of Saccharomyces cerevisiae
    • + channel from the plasma membrane of Saccharomyces cerevisiae. J. Memb. Biol. 132, 183-199.
    • (1993) J. Memb. Biol. , vol.132 , pp. 183-199
    • Bertl, A.1    Slayman, C.L.2    Gradmann, D.3
  • 7
    • 0001423126 scopus 로고
    • + antiporter in membrane vesicles isolated from roots of the halophyte Atriplex nummularia
    • + antiporter in membrane vesicles isolated from roots of the halophyte Atriplex nummularia. Plant Physiol. 87, 104-108.
    • (1988) Plant Physiol. , vol.87 , pp. 104-108
    • Braun, Y.1    Hassidim, M.2    Lerner, H.3    Reinhold, L.4
  • 8
    • 0023218221 scopus 로고
    • Electrochemical potential and ion transport in vesicles of yeast plasma membrane
    • Calahorra, M., Ramirez, J., Clemente, S. M. and Peña. (1987). Electrochemical potential and ion transport in vesicles of yeast plasma membrane. Biochem. Biophys. Acta 899, 229-238.
    • (1987) Biochem. Biophys. Acta , vol.899 , pp. 229-238
    • Calahorra, M.1    Ramirez, J.2    Clemente, S.M.3    Peña4
  • 9
    • 0001436302 scopus 로고
    • + -antiporter in membrane vesicles from oil-seed rape hypocotyls
    • + -antiporter in membrane vesicles from oil-seed rape hypocotyls. Plant Physiol. 97, 1212-1220.
    • (1991) Plant Physiol. , vol.97 , pp. 1212-1220
    • Cooper, S.1    Lemer, H.R.2    Reinhold, L.3
  • 10
    • 0020490954 scopus 로고
    • Active proton uptake in lipid vesicles reconstituted with the purified yeast plasma membrane ATPase. Fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine
    • Dufour, J. P., Goffeau, A. and Tsong, T. Y. (1982). Active proton uptake in lipid vesicles reconstituted with the purified yeast plasma membrane ATPase. Fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine. J. Biol. Chem. 257, 9365-9371.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9365-9371
    • Dufour, J.P.1    Goffeau, A.2    Tsong, T.Y.3
  • 11
    • 0024413230 scopus 로고
    • Optical measurement of membrane potential in cells, organelles, and vesicles
    • Freedman, J. C. and Novak, T. S. (1989). Optical measurement of membrane potential in cells, organelles, and vesicles. Meth. Enzymol. 172, 102-122.
    • (1989) Meth. Enzymol. , vol.172 , pp. 102-122
    • Freedman, J.C.1    Novak, T.S.2
  • 12
    • 0024042922 scopus 로고
    • TRK1 encodes a plasma membrane protein required for high affinity potassium transport in Saccharomyces cerevisiae
    • Gaber, R., Styles, C. and Fink, G. (1988). TRK1 encodes a plasma membrane protein required for high affinity potassium transport in Saccharomyces cerevisiae. Mol. Cell. Biol. 8, 2848-2859.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2848-2859
    • Gaber, R.1    Styles, C.2    Fink, G.3
  • 14
    • 0025785651 scopus 로고
    • Inhibition of glutamate release by arachidonic acid in rat cerebrocortical synaptosomes
    • Herrero, I., Miras-Portugal, M. T. and Sanchez-Prieto, J. (1991). Inhibition of glutamate release by arachidonic acid in rat cerebrocortical synaptosomes. J. Neurochem. 57, 718-721.
    • (1991) J. Neurochem. , vol.57 , pp. 718-721
    • Herrero, I.1    Miras-Portugal, M.T.2    Sanchez-Prieto, J.3
  • 15
    • 0017852795 scopus 로고
    • Pyranine as a sensitive pH probe for liposome interiors and surfaces. pH gradients across phospholipids vesicles
    • Kano, K. and Fendler, J. H. (1978). Pyranine as a sensitive pH probe for liposome interiors and surfaces. pH gradients across phospholipids vesicles. Biochim. Biophys. Acta 509, 289-299.
    • (1978) Biochim. Biophys. Acta , vol.509 , pp. 289-299
    • Kano, K.1    Fendler, J.H.2
  • 16
    • 0017688926 scopus 로고
    • Reconstitution and purification of the D-glucose transporter from human erythrocytes
    • Kasahara, M. and Hinkle, P. (1977). Reconstitution and purification of the D-glucose transporter from human erythrocytes. J. Biol. Chem. 252, 7384-7390.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7384-7390
    • Kasahara, M.1    Hinkle, P.2
  • 17
    • 0028005667 scopus 로고
    • 2+-ATPase activity of higher plant membrane preparations in sucrose solutions
    • 2+-ATPase activity of higher plant membrane preparations in sucrose solutions. Plant Cell. Physiol. 35, 697-700.
    • (1994) Plant Cell. Physiol. , vol.35 , pp. 697-700
    • Kasai, M.1    Sawada, S.2
  • 18
    • 0742330597 scopus 로고
    • +-translocating ATPase from the plasma membrane of Phaseolus mungo L. roots
    • +-translocating ATPase from the plasma membrane of Phaseolus mungo L. roots. Plant Cell. Physiol. 28, 19-28.
    • (1987) Plant Cell. Physiol. , vol.28 , pp. 19-28
    • Kasamo, K.1
  • 19
    • 0025822954 scopus 로고
    • + transporters in Saccharomyces cerevisiae
    • + transporters in Saccharomyces cerevisiae. Mol. Cell. Biol. 11, 4266-4273.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4266-4273
    • Ko, C.H.1    Gaber, R.F.2
  • 21
    • 0015236713 scopus 로고
    • Feeding and melting of lipids bilayers and the mode of action of nonactin, valinomycin, and gramicidin
    • Krasne, S., Eisenman, G. and Szabo, G. (1971). Feeding and melting of lipids bilayers and the mode of action of nonactin, valinomycin, and gramicidin. Science 174, 412-415.
    • (1971) Science , vol.174 , pp. 412-415
    • Krasne, S.1    Eisenman, G.2    Szabo, G.3
  • 22
    • 0027507306 scopus 로고
    • A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport
    • Marger, M. D. and Saier, M. H. (1993). A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport. T.I.B.S. 18, 13-20.
    • (1993) T.I.B.S. , vol.18 , pp. 13-20
    • Marger, M.D.1    Saier, M.H.2
  • 23
    • 0027980905 scopus 로고
    • Cloning and expression of the MEP1 gene encoding an ammonium transporter in Saccharomyces cerevisiae
    • Marini, A. M., Vissers, S., Urrestarazu, A. and Andre, B. (1994). Cloning and expression of the MEP1 gene encoding an ammonium transporter in Saccharomyces cerevisiae. EMBO J. 13, 3456-3463.
    • (1994) EMBO J. , vol.13 , pp. 3456-3463
    • Marini, A.M.1    Vissers, S.2    Urrestarazu, A.3    Andre, B.4
  • 24
    • 0027975568 scopus 로고
    • Membrane potential-dependent calcium transport in right-side-out plasma membrane vesicles from Zea mays L roots
    • Marshall, J., Corzo, A., Leigh, R. and Sanders, D. (1994). Membrane potential-dependent calcium transport in right-side-out plasma membrane vesicles from Zea mays L roots. Plant J. 5, 683-694.
    • (1994) Plant J. , vol.5 , pp. 683-694
    • Marshall, J.1    Corzo, A.2    Leigh, R.3    Sanders, D.4
  • 25
    • 0024963081 scopus 로고
    • Sidedness of yeast plasma membrane vesicles and mechanisms of activation of the ATPase by detergents
    • Monk, B., Montesinos, C., Leonard, K. and Serrano, R. (1989). Sidedness of yeast plasma membrane vesicles and mechanisms of activation of the ATPase by detergents. Biochim. Biophys. Acta 981, 226-234.
    • (1989) Biochim. Biophys. Acta , vol.981 , pp. 226-234
    • Monk, B.1    Montesinos, C.2    Leonard, K.3    Serrano, R.4
  • 26
    • 0023268078 scopus 로고
    • Glucose transport in vesicles reconstituted from Saccharomyces cerevisiae membranes and liposomes
    • Ongjoco, R., Szkutnicka, K. and Cirillo, V. (1987). Glucose transport in vesicles reconstituted from Saccharomyces cerevisiae membranes and liposomes. J. Bacteriol. 169, 2926-2931.
    • (1987) J. Bacteriol. , vol.169 , pp. 2926-2931
    • Ongjoco, R.1    Szkutnicka, K.2    Cirillo, V.3
  • 27
    • 0018447316 scopus 로고
    • Physico-chemical basis of ion transport through biological membranes: Ionophores and ions channels
    • Ovchinnikov, Y. A. (1979). Physico-chemical basis of ion transport through biological membranes: ionophores and ions channels. Eur. J. Biochem. 94, 321-336.
    • (1979) Eur. J. Biochem. , vol.94 , pp. 321-336
    • Ovchinnikov, Y.A.1
  • 28
    • 0021280111 scopus 로고
    • + translocation by the plasma membrane ATPase of Neurospora. Studies on plasma membrane vesicles and reconstituted enzyme
    • + translocation by the plasma membrane ATPase of Neurospora. Studies on plasma membrane vesicles and reconstituted enzyme. J. Biol Chem. 259, 7884-7892.
    • (1984) J. Biol Chem. , vol.259 , pp. 7884-7892
    • Perlin, D.1    Kasamo, L.2    Broocker, R.3    Slayman, C.4
  • 29
    • 0028008822 scopus 로고
    • TRK2 is not a low-affinity potassium transporter in Saccharomyces cerevisiae
    • Ramos, J., Alijo, R., Haro, R. and Rodriguez-Navarro, A. (1994). TRK2 is not a low-affinity potassium transporter in Saccharomyces cerevisiae. J. Bacteriol. 176, 249-252.
    • (1994) J. Bacteriol. , vol.176 , pp. 249-252
    • Ramos, J.1    Alijo, R.2    Haro, R.3    Rodriguez-Navarro, A.4
  • 30
    • 0022404475 scopus 로고
    • A potassium transport mutant of Saccharomyces cerevisiae
    • Ramos, J., Contreras, P. and Rodriguez-Navarro, A. (1985). A potassium transport mutant of Saccharomyces cerevisiae. Arch. Microbiol. 143, 88-93.
    • (1985) Arch. Microbiol. , vol.143 , pp. 88-93
    • Ramos, J.1    Contreras, P.2    Rodriguez-Navarro, A.3
  • 31
    • 0025119613 scopus 로고
    • Regulation of potassium fluxes in Saccharomyces cerevisiae
    • Ramos, J., Haro, R. and Rodriguez-Navarro, A. (1990). Regulation of potassium fluxes in Saccharomyces cerevisiae. Biochim. Biophys Acta 1029, 211-217.
    • (1990) Biochim. Biophys Acta , vol.1029 , pp. 211-217
    • Ramos, J.1    Haro, R.2    Rodriguez-Navarro, A.3
  • 32
    • 0021143010 scopus 로고
    • Dual system for potassium transport in Saccharomyces cerevisiae
    • Rodriguez-Navarro, A. and Ramos, J. (1984). Dual system for potassium transport in Saccharomyces cerevisiae. J. Bacteriol. 159, 940-945.
    • (1984) J. Bacteriol. , vol.159 , pp. 940-945
    • Rodriguez-Navarro, A.1    Ramos, J.2
  • 33
    • 0024517435 scopus 로고
    • Effect of sugar transport inactivation in Saccharomyces cerevisiae on sluggish and stuck enological fermentations
    • Salmon, J. M. (1989). Effect of sugar transport inactivation in Saccharomyces cerevisiae on sluggish and stuck enological fermentations. Appl. Environ. Microbiol. 55, 951-958.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 951-958
    • Salmon, J.M.1
  • 34
    • 0027099840 scopus 로고
    • Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA
    • Schachtman, D. P., Schroeder, J. I., Lucas, W. J., Anderson, J. A. and Gaber, R. F. (1992). Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA. Science 258, 1654-1657.
    • (1992) Science , vol.258 , pp. 1654-1657
    • Schachtman, D.P.1    Schroeder, J.I.2    Lucas, W.J.3    Anderson, J.A.4    Gaber, R.F.5
  • 35
    • 0028114234 scopus 로고
    • Structure and transport mechanism of high-affinity potassium uptake transporter from higher plants
    • Schachtman, D. P. and Schroeder, J. I. (1994). Structure and transport mechanism of high-affinity potassium uptake transporter from higher plants. Nature 370, 655-658.
    • (1994) Nature , vol.370 , pp. 655-658
    • Schachtman, D.P.1    Schroeder, J.I.2
  • 36
    • 0020858948 scopus 로고
    • Purification and reconstitution of the proton-pumping ATPase of fungal and plant plasma membranes
    • Serrano, R. (1983). Purification and reconstitution of the proton-pumping ATPase of fungal and plant plasma membranes. Arch Biochem. 227, 1-8.
    • (1983) Arch Biochem. , vol.227 , pp. 1-8
    • Serrano, R.1
  • 37
    • 0024227621 scopus 로고
    • +-ATPase from plasma membrane of Saccharomyces cerevisiae and A vena saliva roots: Purification and reconstitution
    • +-ATPase from plasma membrane of Saccharomyces cerevisiae and A vena saliva roots: purification and reconstitution. Methods Enzymol. 157, 533-578.
    • (1988) Methods Enzymol. , vol.157 , pp. 533-578
    • Serrano, R.1


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