메뉴 건너뛰기




Volumn 180, Issue 12, 1998, Pages 3131-3136

Altered Na+ and Li+ homeostasis in Saccharomyces cerevisiae cells expressing the bacterial cation antiporter NhaA

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTIPORTER; LITHIUM ION; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SODIUM ION;

EID: 0031782474     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.12.3131-3136.1998     Document Type: Article
Times cited : (25)

References (44)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quatitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quatitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0018564346 scopus 로고
    • Transformation in yeast: Development of a hybrid cloning vector and isolation of the CAN1 gene
    • Broach, J. R., J. N. Strathern, and J. B. Hicks. 1979. Transformation in yeast: development of a hybrid cloning vector and isolation of the CAN1 gene. Gene 8:121-133.
    • (1979) Gene , vol.8 , pp. 121-133
    • Broach, J.R.1    Strathern, J.N.2    Hicks, J.B.3
  • 4
    • 0029166109 scopus 로고
    • Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3
    • Ferrando, A., S. J. Kron, G. Rios, G. R. Fink, and R. Serrano. 1995. Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3. Mol. Cell. Biol. 15:5470-5481.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5470-5481
    • Ferrando, A.1    Kron, S.J.2    Rios, G.3    Fink, G.R.4    Serrano, R.5
  • 5
    • 0026731477 scopus 로고
    • A novel and conserved salt-induced protein is an important determinant of salt tolerance in yeast
    • Gaxiola, R., I. F. Larrinoa, J. M. Villalba, and R. Serrano. 1992. A novel and conserved salt-induced protein is an important determinant of salt tolerance in yeast. EMBO J. 11:3157-3164.
    • (1992) EMBO J. , vol.11 , pp. 3157-3164
    • Gaxiola, R.1    Larrinoa, I.F.2    Villalba, J.M.3    Serrano, R.4
  • 8
    • 0001123955 scopus 로고
    • Mechanisms of salt tolerance in nonhalophytes
    • Greenway, H., and R. Munns. 1980. Mechanisms of salt tolerance in nonhalophytes. Annu. Rev. Plant Physiol. 31:149-190.
    • (1980) Annu. Rev. Plant Physiol. , vol.31 , pp. 149-190
    • Greenway, H.1    Munns, R.2
  • 11
  • 12
    • 0026006263 scopus 로고
    • A novel P-type ATPase from yeast involved in sodium transport
    • Haro, R., B. Garciadeblas, and A. Rodriguez-Navarro. 1991. A novel P-type ATPase from yeast involved in sodium transport. FEBS Lett. 291:189-191.
    • (1991) FEBS Lett. , vol.291 , pp. 189-191
    • Haro, R.1    Garciadeblas, B.2    Rodriguez-Navarro, A.3
  • 13
    • 0025240361 scopus 로고
    • Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+) translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
    • Hirata, R., Y. Ohsumi, A. Nakano, H. Kawasaki, K. Suzuki, and Y. Anraku. 1990. Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+) translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J. Biol. Chem. 265:6726-6733.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6726-6733
    • Hirata, R.1    Ohsumi, Y.2    Nakano, A.3    Kawasaki, H.4    Suzuki, K.5    Anraku, Y.6
  • 15
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 16
    • 0000538964 scopus 로고    scopus 로고
    • Biogenesis and function of the yeast vacuole
    • J. R. Pringle, J. R. Broach, and E. W. Jones (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Jones, E. W., G. C. Webb, and M. A. Hiller. 1997. Biogenesis and function of the yeast vacuole, p. 363-470. In J. R. Pringle, J. R. Broach, and E. W. Jones (ed.), The molecular and cellular biology of the yeast Saccharomyces. Cell cycle and cell biology. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) The Molecular and Cellular Biology of the Yeast Saccharomyces. Cell Cycle and Cell Biology , pp. 363-470
    • Jones, E.W.1    Webb, G.C.2    Hiller, M.A.3
  • 18
    • 0030096580 scopus 로고    scopus 로고
    • Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation
    • Knight, H., A. J. Trewavas, and M. R. Knight. 1996. Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation. Plant Cell 8:489-503.
    • (1996) Plant Cell , vol.8 , pp. 489-503
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 20
    • 0028947362 scopus 로고
    • Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress
    • Luyten, K., J. Albertyn, W. F. Skibbe, B. A. Prior, J. Ramos, J. M. Thevelein, and S. Hohmann. 1995. Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress. EMBO J. 14:1360-1371.
    • (1995) EMBO J. , vol.14 , pp. 1360-1371
    • Luyten, K.1    Albertyn, J.2    Skibbe, W.F.3    Prior, B.A.4    Ramos, J.5    Thevelein, J.M.6    Hohmann, S.7
  • 22
    • 10544225382 scopus 로고    scopus 로고
    • Single point mutations in various domains of a plant plasma membrane H(+)-ATPase expressed in Saccharomyces cerevisiae increase H(+) pumping and permit yeast growth at low pH
    • Morsomme, P., A. de K. d'Exaerde, S. De Meester, D. Thines, A. Goffeau, and M. Boutry. 1996. Single point mutations in various domains of a plant plasma membrane H(+)-ATPase expressed in Saccharomyces cerevisiae increase H(+) pumping and permit yeast growth at low pH. EMBO J. 15: 5513-5526.
    • (1996) EMBO J. , vol.15 , pp. 5513-5526
    • Morsomme, P.1    De D'Exaerde, A.K.2    De Meester, S.3    Thines, D.4    Goffeau, A.5    Boutry, M.6
  • 23
    • 0030704674 scopus 로고    scopus 로고
    • + exchanger in yeast is enhanced by mutations in the plasma membrane ATPase. Insights into mechanisms of sodium tolerance
    • + exchanger in yeast is enhanced by mutations in the plasma membrane ATPase. Insights into mechanisms of sodium tolerance. J. Biol. Chem. 272:26145-26152.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26145-26152
    • Nass, R.1    Cunningham, K.W.2    Rao, R.3
  • 25
    • 77956758262 scopus 로고    scopus 로고
    • + antiporters: Molecular biology, biochemistry and physiology
    • W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Elsevier Science, Amsterdam, The Netherlands
    • + antiporters: molecular biology, biochemistry and physiology, p. 501-531. In W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Handbook of biological physics, vol. 2. Elsevier Science, Amsterdam, The Netherlands.
    • (1996) Handbook of Biological Physics , vol.2 , pp. 501-531
    • Padan, E.1    Schuldiner, S.2
  • 26
    • 0028017842 scopus 로고
    • Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeast
    • Perier, F., K. L. Coulter, H. Liang, C. M. Radeke, R. F. Gaber, and C. A. Vandenberg. 1994. Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeast. FEBS Lett. 351:286-290.
    • (1994) FEBS Lett. , vol.351 , pp. 286-290
    • Perier, F.1    Coulter, K.L.2    Liang, H.3    Radeke, C.M.4    Gaber, R.F.5    Vandenberg, C.A.6
  • 27
    • 0027473930 scopus 로고
    • Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae
    • Perkins, J., and G. M. Gadd. 1993. Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae. FEMS Microbiol. Lett. 107:255-260.
    • (1993) FEMS Microbiol. Lett. , vol.107 , pp. 255-260
    • Perkins, J.1    Gadd, G.M.2
  • 28
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T. A., B. Jungnicker, and U. Kutay. 1996. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65:271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnicker, B.2    Kutay, U.3
  • 30
    • 0000871808 scopus 로고
    • Transport across yeast vacuolar and plasma membranes
    • J. R. Pringle, J. R. Broach, and E. W. Jones (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Serrano, R. 1991. Transport across yeast vacuolar and plasma membranes, p. 523-585. In J. R. Pringle, J. R. Broach, and E. W. Jones (ed.), The molecular and cellular biology of the yeast Saccharomyces. Cell cycle and cell biology. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1991) The Molecular and Cellular Biology of the Yeast Saccharomyces. Cell Cycle and Cell Biology , pp. 523-585
    • Serrano, R.1
  • 31
    • 0029922104 scopus 로고    scopus 로고
    • Salt tolerance in plants and microorganisms: Toxycity targets and defense responses
    • Serrano, R. 1996. Salt tolerance in plants and microorganisms: toxycity targets and defense responses. Int. Rev. Cytol. 165:1-51.
    • (1996) Int. Rev. Cytol. , vol.165 , pp. 1-51
    • Serrano, R.1
  • 32
    • 0029447373 scopus 로고
    • Expression and localization of plant membrane proteins in Saccharomyces
    • Serrano, R., and J. M. Villalba. 1995. Expression and localization of plant membrane proteins in Saccharomyces. Methods Cell Biol. 50:481-496.
    • (1995) Methods Cell Biol. , vol.50 , pp. 481-496
    • Serrano, R.1    Villalba, J.M.2
  • 34
    • 0023705151 scopus 로고
    • The Na, K pump
    • Skou, J. C. 1988. The Na, K pump. Methods Enzymol. 156:1-25.
    • (1988) Methods Enzymol. , vol.156 , pp. 1-25
    • Skou, J.C.1
  • 35
    • 0029618201 scopus 로고
    • Receptor-mediated protein sorting to the vacuole in yeast: Roles for a protein kinase, a lipid kinase and GTP-binding proteins
    • Stack, J. H., B. Horazdovsky, and S. D. Emr. 1995. Receptor-mediated protein sorting to the vacuole in yeast: roles for a protein kinase, a lipid kinase and GTP-binding proteins. Annu. Rev. Cell Dev. Biol. 11:1-33.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 1-33
    • Stack, J.H.1    Horazdovsky, B.2    Emr, S.D.3
  • 40
    • 0001868090 scopus 로고
    • Measurement of fluxes across membranes
    • U. Lüttge, and M. G. Pitman (ed.), Springer Verlag, Berlin, Germany
    • Walker, N. A., and M. G. Pitman. 1976. Measurement of fluxes across membranes, p. 93-117. In U. Lüttge, and M. G. Pitman (ed.), Encyclopedia of plant physiology, new series, vol. 2, part A. Springer Verlag, Berlin, Germany.
    • (1976) Encyclopedia of Plant Physiology, New Series , vol.2 , Issue.PART A , pp. 93-117
    • Walker, N.A.1    Pitman, M.G.2
  • 41
    • 0024324482 scopus 로고
    • A hyper-recombination mutation in S. cerevisae identifies a novel eukaryotic topoisomerase
    • Wallis, J. W., G. Chrebet, G. Brodsky, M. Rolfe, and R. Rothstein. 1989. A hyper-recombination mutation in S. cerevisae identifies a novel eukaryotic topoisomerase. Cell 58:409-419.
    • (1989) Cell , vol.58 , pp. 409-419
    • Wallis, J.W.1    Chrebet, G.2    Brodsky, G.3    Rolfe, M.4    Rothstein, R.5
  • 43
    • 0025362525 scopus 로고
    • Role of vacuolar acidification in protein sorting and zymogen activation: A genetic analysis of the yeast vacuolar protein-translocating ATPase
    • Yamashiro, C. T., P. M. Kane, D. F. Wolczyk, R. A. Preston, and T. H. Stevens. 1990. Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar protein-translocating ATPase. Mol. Cell. Biol. 10:3737-3749.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3737-3749
    • Yamashiro, C.T.1    Kane, P.M.2    Wolczyk, D.F.3    Preston, R.A.4    Stevens, T.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.