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Volumn 437, Issue 2, 2011, Pages 269-278

A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast

Author keywords

Chimaeric membrane protein; Green fluorescent protein; Heterologous expression; Proton translocating inorganic pyrophosphatase; Saccharomyces cerevisiae; Vacuolar type ATPase

Indexed keywords

BAFILOMYCIN; FLUORESCENT DYE; MEPACRINE; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 79959716999     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110447     Document Type: Article
Times cited : (23)

References (45)
  • 3
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007) Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 5
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E. J., Siebers, A. and Altendorf, K. (1988) Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. U.S.A. 85, 7972-7976
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 6
    • 4043065767 scopus 로고    scopus 로고
    • The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae
    • Bowman, E. J., Graham, L. A., Stevens, T. H. and Bowman, B. J. (2004) The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae. J. Biol. Chem. 279, 33131-33138
    • (2004) J. Biol. Chem. , vol.279 , pp. 33131-33138
    • Bowman, E.J.1    Graham, L.A.2    Stevens, T.H.3    Bowman, B.J.4
  • 9
    • 0030788474 scopus 로고    scopus 로고
    • Mutants of Saccharomyces cerevisiae defective in vacuolar function confirm a role for the vacuole in toxic metal ion detoxification
    • Ramsay, L. M. and Gadd, G. M. (1997) Mutants of Saccharomyces cerevisiae defective in vacuolar function confirm a role for the vacuole in toxic metal ion detoxification. FEMS Microbiol. Lett. 152, 293-298
    • (1997) FEMS Microbiol. Lett. , vol.152 , pp. 293-298
    • Ramsay, L.M.1    Gadd, G.M.2
  • 10
    • 62149142874 scopus 로고    scopus 로고
    • V-ATPase functions in normal and disease processes
    • Hinton, A., Bond, S. and Forgac, M. (2009) V-ATPase functions in normal and disease processes. Pflugers Arch. 457, 589-598
    • (2009) Pflugers Arch. , vol.457 , pp. 589-598
    • Hinton, A.1    Bond, S.2    Forgac, M.3
  • 11
    • 0344444207 scopus 로고    scopus 로고
    • + ATPase
    • + ATPase. Biol. Cell 95, 453-457
    • (2003) Biol. Cell , vol.95 , pp. 453-457
    • Morel, N.1
  • 12
    • 0035209342 scopus 로고    scopus 로고
    • + pyrophosphatases: From the evolutionary backwaters into the mainstream
    • + pyrophosphatases: from the evolutionary backwaters into the mainstream. Trends Plant Sci. 6, 206-211
    • (2001) Trends Plant Sci. , vol.6 , pp. 206-211
    • Drozdowicz, Y.M.1    Rea, P.A.2
  • 16
    • 0035805112 scopus 로고    scopus 로고
    • +-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima
    • DOI 10.1016/S0014-5793(01)02390-0, PII S0014579301023900
    • Pérez-Castiñeira, J. R., López-Marqués, R. L., Losada, M. and Serrano, A. (2001) A thermostable K+-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima . FEBS Lett. 496, 6-11 (Pubitemid 32436413)
    • (2001) FEBS Letters , vol.496 , Issue.1 , pp. 6-11
    • Perez-Castineira, J.R.1    Lopez-Marques, R.L.2    Losada, M.3    Serrano, A.4
  • 17
    • 0035469221 scopus 로고    scopus 로고
    • Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: Remnants or metabolic cornerstones?
    • Pérez-Castiñeira, J. R., Gómez-García, R., López-Marqués, R. L., Losada, M. and Serrano, A. (2001) Enzymatic systems of inorganic pyrophosphate bioenergetics in photosynthetic and heterotrophic protists: remnants or metabolic cornerstones? Int. Microbiol. 4, 135-142
    • (2001) Int. Microbiol. , vol.4 , pp. 135-142
    • Pérez-Castiñeira, J.R.1    Gómez-García, R.2    López-Marqués, R.L.3    Losada, M.4    Serrano, A.5
  • 18
    • 33749542773 scopus 로고    scopus 로고
    • Endomembrane proton pumps: Connecting membrane and vesicle transport
    • Schumacher, K. (2006) Endomembrane proton pumps: connecting membrane and vesicle transport. Curr. Opin. Plant Biol. 9, 595-600
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 595-600
    • Schumacher, K.1
  • 19
    • 0028278224 scopus 로고
    • Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport
    • Kim, E. J., Zhen, R. G. and Rea, P. A. (1994) Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport. Proc. Natl. Acad. Sci. U.S.A. 91, 6128-6132
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 6128-6132
    • Kim, E.J.1    Zhen, R.G.2    Rea, P.A.3
  • 20
    • 0034306414 scopus 로고    scopus 로고
    • Cloning and functional expression of a gene encoding a vacuolar-type proton-translocating pyrophosphatase from Trypanosoma cruzi
    • Hill, J. E., Scott, D. A., Luo, S. and Docampo, R. (2000) Cloning and functional expression of a gene encoding a vacuolar-type proton-translocating pyrophosphatase from Trypanosoma cruzi. Biochem. J. 351, 281-288
    • (2000) Biochem. J. , vol.351 , pp. 281-288
    • Hill, J.E.1    Scott, D.A.2    Luo, S.3    Docampo, R.4
  • 21
    • 76549089845 scopus 로고    scopus 로고
    • N-terminal chimaeras with signal sequences enhance the functional expression and alter the subcellular localization of heterologous membrane-bound inorganic pyrophosphatases in yeast
    • Drake, R., Serrano, A. and Pérez-Castiñeira, J. R. (2010) N-terminal chimaeras with signal sequences enhance the functional expression and alter the subcellular localization of heterologous membrane-bound inorganic pyrophosphatases in yeast. Biochem. J. 426, 147-157
    • (2010) Biochem. J. , vol.426 , pp. 147-157
    • Drake, R.1    Serrano, A.2    Pérez-Castiñeira, J.R.3
  • 22
    • 0031782474 scopus 로고    scopus 로고
    • + homeostasis in Saccharomyces cerevisiae cells expressing the bacterial cation antiporter NhaA
    • Ros, R., Montesinos, C., Rimon, A., Padan, E. and Serrano, R. (1998) Altered Na+ and Li+ homeostasis in Saccharomyces cerevisiae cells expressing the bacterial cation antiporter NhaA. J. Bacteriol. 180, 3131-3136 (Pubitemid 28285026)
    • (1998) Journal of Bacteriology , vol.180 , Issue.12 , pp. 3131-3136
    • Ros, R.1    Montesinos, C.2    Rimon, A.3    Padan, E.4    Serrano, R.5
  • 24
    • 0025974219 scopus 로고
    • Tackling the protease problem in Saccharomyces cerevisiae
    • Jones, E. W. (1991) Tackling the protease problem in Saccharomyces cerevisiae. Methods Enzymol. 194, 428-453
    • (1991) Methods Enzymol. , vol.194 , pp. 428-453
    • Jones, E.W.1
  • 25
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R. H. and Gietz, R. D. (1989) High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16, 339-346
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 26
    • 0036500159 scopus 로고    scopus 로고
    • +and pH homeostasis: Implications for salt tolerance, cell wall integrity and cell cycle progression
    • + and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression. EMBO J. 21, 920-929
    • (2002) EMBO J. , vol.21 , pp. 920-929
    • Yenush, L.1    Mulet, J.M.2    Arino, J.3    Serrano, R.4
  • 32
    • 0014663389 scopus 로고
    • Estimation of enzymically produced orthophosphate in the presence of cysteine and adenosine triphosphate
    • Rathbun, W. B. and Betlach, M. V. (1969) Estimation of enzymically produced orthophosphate in the presence of cysteine and adenosine triphosphate. Anal. Biochem. 28, 436-445
    • (1969) Anal. Biochem. , vol.28 , pp. 436-445
    • Rathbun, W.B.1    Betlach, M.V.2
  • 33
    • 0025054113 scopus 로고
    • +-ATPase of adrenal secretory granulesRapid partial purification and reconstitution into proteoliposomes
    • +-ATPase of adrenal secretory granulesRapid partial purification and reconstitution into proteoliposomes. Biochem. J. 271, 127-131
    • (1990) Biochem. J. , vol.271 , pp. 127-131
    • Pérez-Castiñeira, J.R.1    Apps, D.K.2
  • 34
    • 0030855218 scopus 로고    scopus 로고
    • Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. Strain PCC 6803
    • Valverde, F., Losada, M. and Serrano, A. (1997) Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. J. Bacteriol. 179, 4513-4522 (Pubitemid 27299067)
    • (1997) Journal of Bacteriology , vol.179 , Issue.14 , pp. 4513-4522
    • Valverde, F.1    Losada, M.2    Serrano, A.3
  • 35
    • 25444451062 scopus 로고    scopus 로고
    • Large-scale purification of the proton pumping pyrophosphatase from Thermotoga maritima: A 'Hot-Solve' method for isolation of recombinant thermophilic membrane proteins
    • López-Marqués, R. L., Pérez-Castiñeira, J. R., Buch-Pedersen, M. J., Marco, S., Rigaud, J. L., Palmgren, M. G. and Serrano, A. (2005) Large-scale purification of the proton pumping pyrophosphatase from Thermotoga maritima : a 'Hot-Solve' method for isolation of recombinant thermophilic membrane proteins. Biochim. Biophys. Acta 1716, 69-76
    • (2005) Biochim. Biophys. Acta , vol.1716 , pp. 69-76
    • López-Marqués, R.L.1    Pérez-Castiñeira, J.R.2    Buch-Pedersen, M.J.3    Marco, S.4    Rigaud, J.L.5    Palmgren, M.G.6    Serrano, A.7
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation 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
  • 37
    • 0036022310 scopus 로고    scopus 로고
    • Characterization of yeast V-ATPase mutants lacking Vph1p or Stv1p and the effect on endocytosis
    • Perzov, N., Padler-Karavani, V., Nelson, H. and Nelson, N. (2002) Characterization of yeast V-ATPase mutants lacking Vph1p or Stv1p and the effect on endocytosis. J. Exp. Biol. 205, 1209-1219
    • (2002) J. Exp. Biol. , vol.205 , pp. 1209-1219
    • Perzov, N.1    Padler-Karavani, V.2    Nelson, H.3    Nelson, N.4
  • 38
    • 34548813656 scopus 로고    scopus 로고
    • Structure of acid-sensing ion channel 1 at 1.9 Å resolution and low pH
    • DOI 10.1038/nature06163, PII NATURE06163
    • Jasti, J., Furukawa, H., Gonzales, E. B. and Gouaux, E. (2007) Structure of acid-sensing ion channel 1 at 1.9 Å resolution and low pH. Nature 449, 316-323 (Pubitemid 47443482)
    • (2007) Nature , vol.449 , Issue.7160 , pp. 316-323
    • Jasti, J.1    Furukawa, H.2    Gonzales, E.B.3    Gouaux, E.4
  • 39
    • 0035809932 scopus 로고    scopus 로고
    • Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer
    • DOI 10.1083/jcb.152.5.935
    • Sato, K., Sato, M. and Nakano, A. (2001) Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomer. J. Cell Biol. 152, 935-944 (Pubitemid 34286070)
    • (2001) Journal of Cell Biology , vol.152 , Issue.5 , pp. 935-944
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 40
    • 0025856178 scopus 로고
    • Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme?
    • Mertens, E. (1991) Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme? FEBS Lett. 285, 1-5
    • (1991) FEBS Lett. , vol.285 , pp. 1-5
    • Mertens, E.1
  • 41
    • 34948873616 scopus 로고    scopus 로고
    • Role of the V-ATPase in regulation of the vacuolar fission-fusion equilibrium
    • Baars, T. L., Petri, S., Peters, C. and Mayer, A. (2007) Role of the V-ATPase in regulation of the vacuolar fission-fusion equilibrium. Mol. Biol. Cell 18, 3873-3882
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3873-3882
    • Baars, T.L.1    Petri, S.2    Peters, C.3    Mayer, A.4
  • 42
    • 34248204178 scopus 로고    scopus 로고
    • Plant proton pumps
    • DOI 10.1016/j.febslet.2007.03.050, PII S0014579307003225, Plant Transporters and Channels
    • Gaxiola, R. A., Palmgren, M. G. and Schumacher, K. (2007) Plant proton pumps. FEBS Lett. 581, 2204-2214 (Pubitemid 46726301)
    • (2007) FEBS Letters , vol.581 , Issue.12 , pp. 2204-2214
    • Gaxiola, R.A.1    Palmgren, M.G.2    Schumacher, K.3
  • 43
    • 3843077423 scopus 로고    scopus 로고
    • Differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics
    • DOI 10.1128/JB.186.16.5418-5426.2004
    • López-Marqués, R. L., Pérez-Castiñeira, J. R., Losada, M. and Serrano, A. (2004) Differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics. J. Bacteriol. 186, 5418-5426 (Pubitemid 39038143)
    • (2004) Journal of Bacteriology , vol.186 , Issue.16 , pp. 5418-5426
    • Lopez-Marques, R.L.1    Perez-Castineira, J.R.2    Losada, M.3    Serrano, A.4
  • 44
    • 77949536638 scopus 로고    scopus 로고
    • Purification and functional characterization of protoplasts and intact vacuoles from grape cells
    • Fontes, N., Silva, R., Vignault, C., Lecourieux, F., Geros, H. and Delrot, S. (2010) Purification and functional characterization of protoplasts and intact vacuoles from grape cells. BMC Res. Notes 3, 19
    • (2010) BMC Res. Notes , vol.3 , pp. 19
    • Fontes, N.1    Silva, R.2    Vignault, C.3    Lecourieux, F.4    Geros, H.5    Delrot, S.6
  • 45
    • 0036298085 scopus 로고    scopus 로고
    • Evidence for a wide occurrence of proton-translocating pyrophosphatase genes in parasitic and free-living protozoa
    • Pérez-Castiñeira, J. R., Alvar, J., Ruíz- Pérez, L. M. and Serrano, A. (2002) Evidence for a wide occurrence of proton-translocating pyrophosphatase genes in parasitic and free-living protozoa. Biochem. Biophys. Res. Commun. 294, 567-573
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 567-573
    • Pérez-Castiñeira, J.R.1    Alvar, J.2    Ruíz-Pérez, L.M.3    Serrano, A.4


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