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Volumn 186, Issue 16, 2004, Pages 5418-5426

Differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; INORGANIC PYROPHOSPHATASE; MEMBRANE BOUND INORGANIC PYROHOSPHATASE; PYROPHOSPHATE; REGA PROTEIN; SOLUBLE INORGANIC PYROPHOSPHATASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 3843077423     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.16.5418-5426.2004     Document Type: Article
Times cited : (41)

References (60)
  • 3
    • 0014004370 scopus 로고
    • Inorganic pyrophosphate formation in bacterial photophosphorylation
    • Baltscheffsky, H., L. V. Von Steding, H. W. Heldt, and M. Klingenberg. 1966. Inorganic pyrophosphate formation in bacterial photophosphorylation. Science 153:1120-1124.
    • (1966) Science , vol.153 , pp. 1120-1124
    • Baltscheffsky, H.1    Von Steding, L.V.2    Heldt, H.W.3    Klingenberg, M.4
  • 5
    • 0031806558 scopus 로고    scopus 로고
    • A pyrophosphate synthase gene: Molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum
    • Baltscheffsky, M., S. Nadanaciva, and A. Schultz. 1998. A pyrophosphate synthase gene: molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum. Biochim. Biophys. Acta 1364:301-306.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 301-306
    • Baltscheffsky, M.1    Nadanaciva, S.2    Schultz, A.3
  • 6
    • 0023938869 scopus 로고
    • Analysis of the Rhodobacter capsulatus puf operon: Location of the oxygen-regulated promoter region and the identification of an additional puf-encoded gene
    • Bauer, C. E., D. A. Young, and B. L. Marrs. 1988. Analysis of the Rhodobacter capsulatus puf operon: location of the oxygen-regulated promoter region and the identification of an additional puf-encoded gene. J. Biol. Chem. 263:4820-4827.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4820-4827
    • Bauer, C.E.1    Young, D.A.2    Marrs, B.L.3
  • 7
    • 0032724622 scopus 로고    scopus 로고
    • Mechanisms for redox control of gene expression
    • Bauer, C. E., S. Elsen, and T. H. Bird. 1999. Mechanisms for redox control of gene expression. Annu. Rev. Microbiol. 53:495-523.
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 495-523
    • Bauer, C.E.1    Elsen, S.2    Bird, T.H.3
  • 8
    • 18744423090 scopus 로고    scopus 로고
    • Identification and analysis of proton-translocating pyrophosphatases in the methanogenic archaeon Methanosarcina mazei
    • Bäumer, S., S. Lentes, G. Gottschalk, and U. Deppenmeier. 2002. Identification and analysis of proton-translocating pyrophosphatases in the methanogenic archaeon Methanosarcina mazei. Archaea 1:1-7.
    • (2002) Archaea , vol.1 , pp. 1-7
    • Bäumer, S.1    Lentes, S.2    Gottschalk, G.3    Deppenmeier, U.4
  • 9
    • 0036837743 scopus 로고    scopus 로고
    • Transcription activation by FNR: Evidence for a functional activating region 2
    • Blake, T., A. Barnard, S. J. W. Bushy, and J. Green. 2002. Transcription activation by FNR: evidence for a functional activating region 2. J. Bacteriol. 184:5855-5861.
    • (2002) J. Bacteriol. , vol.184 , pp. 5855-5861
    • Blake, T.1    Barnard, A.2    Bushy, S.J.W.3    Green, J.4
  • 10
    • 0346271736 scopus 로고
    • Light-activated hydrogenase activity in a photosynthetic bacterium: A permeability phenomenon
    • Bose, S. K., H. Gest, and J. G. Ormerod. 1961. Light-activated hydrogenase activity in a photosynthetic bacterium: a permeability phenomenon. J. Biol. Chem. 236:PC13-PC14.
    • (1961) J. Biol. Chem. , vol.236
    • Bose, S.K.1    Gest, H.2    Ormerod, J.G.3
  • 11
    • 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
  • 13
    • 0001895754 scopus 로고
    • Absorption spectra of photosynthetic bacteria and their chlorophylls
    • H. Gest, A. San Pietro, and L. P. Vernon (ed.). Antioch Press, Yellow Springs, Ohio
    • Clayton, R. K. 1963. Absorption spectra of photosynthetic bacteria and their chlorophylls, p. 495-500. In H. Gest, A. San Pietro, and L. P. Vernon (ed.), Bacterial photosynthesis. Antioch Press, Yellow Springs, Ohio.
    • (1963) Bacterial Photosynthesis , pp. 495-500
    • Clayton, R.K.1
  • 14
    • 0006200926 scopus 로고
    • The fine structure of Rhodospirillum rubrum cell
    • Cohen-Bazire, G., and R. Kunisawa. 1963. The fine structure of Rhodospirillum rubrum cell. J. Cell Biol. 16:401-419.
    • (1963) J. Cell Biol. , vol.16 , pp. 401-419
    • Cohen-Bazire, G.1    Kunisawa, R.2
  • 15
    • 70449138041 scopus 로고
    • Kinetic studies of pigment synthesis by nonsulfur purple bacteria
    • Cohen-Bazire, G., W. R. Sistrom, and R. Y. Stanier. 1957. Kinetic studies of pigment synthesis by nonsulfur purple bacteria. J. Cell. Comp. Physiol. 49:25-68.
    • (1957) J. Cell. Comp. Physiol. , vol.49 , pp. 25-68
    • Cohen-Bazire, G.1    Sistrom, W.R.2    Stanier, R.Y.3
  • 16
    • 0001047476 scopus 로고
    • Enhanced activity of tonoplast pyrophosphatase in NaCl grown cells of Daucus carota
    • Colomho, R., and R. Cerana. 1993. Enhanced activity of tonoplast pyrophosphatase in NaCl grown cells of Daucus carota. J. Plant Physiol. 142:226-229.
    • (1993) J. Plant Physiol. , vol.142 , pp. 226-229
    • Colomho, R.1    Cerana, R.2
  • 17
    • 0028837363 scopus 로고
    • Chill-induced changes in the activity and abundance of the vacuolar proton-pumping pyrophosphatase from Mung bean hypocotyls
    • Darley, C. P., J. M. Davies, and D. Sanders. 1995. Chill-induced changes in the activity and abundance of the vacuolar proton-pumping pyrophosphatase from Mung bean hypocotyls. Plant Physiol. 109:659-665.
    • (1995) Plant Physiol. , vol.109 , pp. 659-665
    • Darley, C.P.1    Davies, J.M.2    Sanders, D.3
  • 19
    • 0035209342 scopus 로고    scopus 로고
    • Vacuolar H+ pyrophosphatase: From the evolutionary backwaters into the mainstream
    • Drozdowicz, Y. M., and P. A. Rea. 2001. Vacuolar H+ pyrophosphatase: 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
  • 20
    • 0032725586 scopus 로고    scopus 로고
    • A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: Implications for the origins of pyrophosphate-energized pumps
    • Drozdowicz, Y. M., Y.-P. Lu, V. Patel, S. Fitz-Gibbon, J. H. Miller, and P. A. Rea. 1999. A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: implications for the origins of pyrophosphate-energized pumps. FEBS Lett. 460:505-512.
    • (1999) FEBS Lett. , vol.460 , pp. 505-512
    • Drozdowicz, Y.M.1    Lu, Y.-P.2    Patel, V.3    Fitz-Gibbon, S.4    Miller, J.H.5    Rea, P.A.6
  • 21
    • 0032541134 scopus 로고    scopus 로고
    • DNA binding characteristics of RegA: A constitutively active anaerobic activator of photosynthetic gene expression in Rhodobacter capsulatus
    • Du, S., T. H. Bird, and C. E. Bauer. 1998. DNA binding characteristics of RegA: a constitutively active anaerobic activator of photosynthetic gene expression in Rhodobacter capsulatus. J. Biol. Chem. 273:18509-18513.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18509-18513
    • Du, S.1    Bird, T.H.2    Bauer, C.E.3
  • 23
    • 0036374202 scopus 로고    scopus 로고
    • Expression studies of two paralogous ppa genes encoding distinct family I pyrophosphatases in marine unicellular cyanobacteria reveal inactivation of the typical cyanobacterial gene
    • Gómez-García, M. R., and A. Serrano. 2002. Expression studies of two paralogous ppa genes encoding distinct family I pyrophosphatases in marine unicellular cyanobacteria reveal inactivation of the typical cyanobacterial gene. Biochem. Biophys. Res. Commun. 295:890-897.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 890-897
    • Gómez-García, M.R.1    Serrano, A.2
  • 24
    • 0037436832 scopus 로고    scopus 로고
    • Concurrent transcriptional activation of ppa and ppx genes by phosphate deprivation in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Gómez-Garría, M. R., M. Losada, and A. Serrano. 2003. Concurrent transcriptional activation of ppa and ppx genes by phosphate deprivation in the cyanobacterium Synechocystis sp. strain PCC 6803. Biochem. Biophys. Res. Commun. 302:284-292.
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 284-292
    • Gómez-Garría, M.R.1    Losada, M.2    Serrano, A.3
  • 26
    • 0029855868 scopus 로고    scopus 로고
    • A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation
    • Joshi, H. M., and F. R. Tabita. 1996. A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation. Proc. Natl. Acad. Sci. USA 93:14515-14520.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14515-14520
    • Joshi, H.M.1    Tabita, F.R.2
  • 28
    • 0025971039 scopus 로고
    • A short procedure for Southern blotting on neutral and anionic membranes
    • Kempter, B., P. Luppo, and D. Neumeier. 1991. A short procedure for Southern blotting on neutral and anionic membranes. Trends Genet. 7:109-110.
    • (1991) Trends Genet. , vol.7 , pp. 109-110
    • Kempter, B.1    Luppo, P.2    Neumeier, D.3
  • 29
    • 0015043627 scopus 로고
    • Regulatory properties of an inorganic pyrophosphatase from the photosynthetic bacterium Rhodospirillum rubrum
    • Klemme, J.-H., and H. Gest. 1971. Regulatory properties of an inorganic pyrophosphatase from the photosynthetic bacterium Rhodospirillum rubrum. Proc. Natl. Acad. Sci. USA 68:721-725.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 721-725
    • Klemme, J.-H.1    Gest, H.2
  • 30
    • 0015241489 scopus 로고
    • Regulation of the cytoplasmic inorganic pyrophosphatase of Rhodospirillum rubrum
    • Klemme, J. H., and H. Gest. 1971. Regulation of the cytoplasmic inorganic pyrophosphatase of Rhodospirillum rubrum. Eur. J. Biochem. 22:529-537.
    • (1971) Eur. J. Biochem. , vol.22 , pp. 529-537
    • Klemme, J.H.1    Gest, H.2
  • 31
    • 0021959540 scopus 로고
    • Inorganic pyrophosphate and inorganic pyrophosphatases in Escherichia coli
    • Kukko-Kalse, E., and J. Heinonen. 1985. Inorganic pyrophosphate and inorganic pyrophosphatases in Escherichia coli. Int. J. Biochem. 17:575-580.
    • (1985) Int. J. Biochem. , vol.17 , pp. 575-580
    • Kukko-Kalse, E.1    Heinonen, J.2
  • 32
    • 0024720464 scopus 로고
    • Intracellular PPi concentration is not directly dependent on amount of inorganic pyrophosphatase in Escherichia coli K-12 cells
    • Kukko-Kalse, E., M. Lintunen, M. K. Inen, R. Lahti, and J. Heinonen. 1989. Intracellular PPi concentration is not directly dependent on amount of inorganic pyrophosphatase in Escherichia coli K-12 cells. J. Bacteriol. 171:4498-4500.
    • (1989) J. Bacteriol. , vol.171 , pp. 4498-4500
    • Kukko-Kalse, E.1    Lintunen, M.2    Inen, M.K.3    Lahti, R.4    Heinonen, J.5
  • 33
    • 0344237366 scopus 로고    scopus 로고
    • Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: Insights into DNA binding specificity
    • Laguri, C., M. K. Phillips-Jones, and M. P. Williamson. 2003. Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity. Nucleic Acids Res. 31:6778-6787.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6778-6787
    • Laguri, C.1    Phillips-Jones, M.K.2    Williamson, M.P.3
  • 34
    • 0024233964 scopus 로고
    • Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12
    • Lahti, R., T. Pitkäranta, E. Valve, I. Ilta, E. Kukko-Kalse, and J. Heinonen. 1988. Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12. J. Bacteriol. 170:5901-5907.
    • (1988) J. Bacteriol. , vol.170 , pp. 5901-5907
    • Lahti, R.1    Pitkäranta, T.2    Valve, E.3    Ilta, I.4    Kukko-Kalse, E.5    Heinonen, J.6
  • 35
    • 3843137513 scopus 로고
    • Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from Mung bean
    • Maeshima, M., and S. Yoshida. 1989. Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from Mung bean. J. Biol. Chem. 196:11-17.
    • (1989) J. Biol. Chem. , vol.196 , pp. 11-17
    • Maeshima, M.1    Yoshida, S.2
  • 36
    • 3843073394 scopus 로고
    • Modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A., S. M. Haas, L. L. Bieber, and N. E. Tolhert. 1987. Modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 180:152-157.
    • (1987) Anal. Biochem. , vol.180 , pp. 152-157
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolhert, N.E.4
  • 39
    • 0036015648 scopus 로고    scopus 로고
    • Mutual dependence of the expression of the cell differentiation regulatory protein HetR and the global nitrogen regulator NtcA during heterocyst development
    • Muro-Pastor, A. M., A. Valladares, E. Flores, and A. Herrero. 2002. Mutual dependence of the expression of the cell differentiation regulatory protein HetR and the global nitrogen regulator NtcA during heterocyst development. Mol. Microbiol. 44:1377-1385.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1377-1385
    • Muro-Pastor, A.M.1    Valladares, A.2    Flores, E.3    Herrero, A.4
  • 40
    • 3843084233 scopus 로고    scopus 로고
    • +-pyrophosphatase and its developmental expression in growing hypocotyl of Mung bean
    • +-pyrophosphatase and its developmental expression in growing hypocotyl of Mung bean. Plant Physiol. 100:718-722.
    • (1998) Plant Physiol. , vol.100 , pp. 718-722
    • Nakanishi, Y.1    Maeshima, M.2
  • 41
    • 0026026887 scopus 로고
    • Hypothesis: The physiological role of the membrane-bound proton-translocating pyrophosphatase of some phototrophic bacteria
    • Nyrén, P., and Å. Strid. 1991. Hypothesis: the physiological role of the membrane-bound proton-translocating pyrophosphatase of some phototrophic bacteria. FEMS Microbiol. Lett. 77:265-270.
    • (1991) FEMS Microbiol. Lett. , vol.77 , pp. 265-270
    • Nyrén, P.1    Strid, Å.2
  • 42
    • 0025752365 scopus 로고
    • Proton-pumping N,N′-dicyclohexylcarbodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum: Purification, characterization and reconstitution
    • Nyrén, P., B. F. Nore, and Å. Strid. 1991. Proton-pumping N,N′-dicyclohexylcarbodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum: purification, characterization and reconstitution. Biochemistry 30:2883-2887.
    • (1991) Biochemistry , vol.30 , pp. 2883-2887
    • Nyrén, P.1    Nore, B.F.2    Strid, Å.3
  • 43
    • 0017077695 scopus 로고
    • Early formation of intracytoplasmic membranes in Rhodospirillum rubrum
    • Oelze, J. 1976. Early formation of intracytoplasmic membranes in Rhodospirillum rubrum. Biochim. Biophys. Acta 436:95-100.
    • (1976) Biochim. Biophys. Acta , vol.436 , pp. 95-100
    • Oelze, J.1
  • 44
    • 0036298085 scopus 로고    scopus 로고
    • Evidence for the wide occurrence of proton-translocating pyrophosphatase genes in parasitic and free-living protozoa
    • Pérez-Castiñeira, J. R., J. Alvar, L. M. Ruiz-Pérez, and A. Serrano. 2002. Evidence for the 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    Ruiz-Pérez, L.M.3    Serrano, A.4
  • 46
    • 0030046502 scopus 로고    scopus 로고
    • 2 fixation in Rhodobacter sphaeroides
    • 2 fixation in Rhodobacter sphaeroides. J. Bacteriol. 178:12-18.
    • (1996) J. Bacteriol. , vol.178 , pp. 12-18
    • Qian, Y.1    Tabita, F.R.2
  • 47
    • 0018593101 scopus 로고
    • Characterization of the membrane-bound inorganic pyrophosphatase in Rhodospirillum rubrum
    • Randahl, H. 1979. Characterization of the membrane-bound inorganic pyrophosphatase in Rhodospirillum rubrum. Eur. J. Biochem. 102:251-256.
    • (1979) Eur. J. Biochem. , vol.102 , pp. 251-256
    • Randahl, H.1
  • 50
    • 0026052188 scopus 로고
    • A membrane-bound pyrophosphatase from respiratory membranes of Rhodospirillum rubrum
    • Romero, I., A. Gómez-Priego, and H. Celis. 1991. A membrane-bound pyrophosphatase from respiratory membranes of Rhodospirillum rubrum. J. Gen. Microbiol. 137:2611-2616.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2611-2616
    • Romero, I.1    Gómez-Priego, A.2    Celis, H.3
  • 51
    • 0026512325 scopus 로고
    • Molecular cloning and sequence of cDNA encoding the pyrophosphate- energized vacuolar-membrane proton-pump of Arabidopsis thaliana
    • Sarafian, V., Y. Kim, R. J. Poole, and P. A. Rea. 1992. Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar-membrane proton-pump of Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 89:1775-1779.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1775-1779
    • Sarafian, V.1    Kim, Y.2    Poole, R.J.3    Rea, P.A.4
  • 52
    • 0020077920 scopus 로고
    • Fermentation and anaerobic respiration by Rhodospirillum rubrum and Rhodopseudomonas capsulata
    • Schultz, J. E., and P. F. Weaver. 1982. Fermentation and anaerobic respiration by Rhodospirillum rubrum and Rhodopseudomonas capsulata. J. Bacteriol. 149:181-190.
    • (1982) J. Bacteriol. , vol.149 , pp. 181-190
    • Schultz, J.E.1    Weaver, P.F.2
  • 53
    • 0042154176 scopus 로고    scopus 로고
    • Identification of organelles in bacteria similar to acidocalcisomes of unicellular eukaryotes
    • Seufferheld, M., M. C. F. Vieira, F. A. Ruiz, C. O. Rodrigues, S. N. J. Moreno, and R. Docampo. 2003. Identification of organelles in bacteria similar to acidocalcisomes of unicellular eukaryotes. J. Biol. Chem. 278:29971-29978.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29971-29978
    • Seufferheld, M.1    Vieira, M.C.F.2    Ruiz, F.A.3    Rodrigues, C.O.4    Moreno, S.N.J.5    Docampo, R.6
  • 54
    • 38249033324 scopus 로고
    • Demonstration of ApH and ΔΨ-induced synthesis of inorganic pyrophosphate in chromatophores from Rhodospirillum rubrum
    • Strid, Å., I.-M. Karlsson, and M. Baltscheffsky. 1987. Demonstration of ApH and ΔΨ-induced synthesis of inorganic pyrophosphate in chromatophores from Rhodospirillum rubrum. FEBS Lett. 224:348-352.
    • (1987) FEBS Lett. , vol.224 , pp. 348-352
    • Strid, Å.1    Karlsson, I.-M.2    Baltscheffsky, M.3
  • 55
    • 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., M. Losada, and A. Serrano. 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.
    • (1997) J. Bacteriol. , vol.179 , pp. 4513-4522
    • Valverde, F.1    Losada, M.2    Serrano, A.3
  • 56
    • 0037244432 scopus 로고    scopus 로고
    • Specialized osmotic stress response systems involve multiple SigB-like sigma factors in Streptomyces coelicolor
    • Viollier, P. H., G. H. Kelemen, G. E. Dale, K. T. Nguyen, M. J. Buttner, and C. J. Thompson. 2003. Specialized osmotic stress response systems involve multiple SigB-like sigma factors in Streptomyces coelicolor. Mol. Microbiol. 47:699-714.
    • (2003) Mol. Microbiol. , vol.47 , pp. 699-714
    • Viollier, P.H.1    Kelemen, G.H.2    Dale, G.E.3    Nguyen, K.T.4    Buttner, M.J.5    Thompson, C.J.6
  • 57
    • 0001197431 scopus 로고
    • Subcellular compartmentation of pyrophosphate and alkaline pyrophosphatase in leaves
    • Weiner, H., M. Stitt, and H. W. Heldt. 1987. Subcellular compartmentation of pyrophosphate and alkaline pyrophosphatase in leaves. Biochim. Biophys. Acta 893:13-21.
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 13-21
    • Weiner, H.1    Stitt, M.2    Heldt, H.W.3
  • 58
    • 0035108157 scopus 로고    scopus 로고
    • Salt-stress-responsive membrane proteins in Rhodobacter sphaeroides f. sp. denitrificans IL106
    • Xu, X., M. Abo, A. Okubo, and S. Yamakazi. 2001. Salt-stress-responsive membrane proteins in Rhodobacter sphaeroides f. sp. denitrificans IL106. J. Biosci. Bioeng. 91:228-230.
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 228-230
    • Xu, X.1    Abo, M.2    Okubo, A.3    Yamakazi, S.4
  • 59
    • 0034888605 scopus 로고    scopus 로고
    • Cloning and sequencing of a gene encoding a novel salt stress-induced membrane protein from Rhodobacter sphaeroides f. sp. denitrificans
    • Xu, X. Y., H. Kadokura, A. Okubo, K. Kitamoto, and S. Yamakazi. 2001. Cloning and sequencing of a gene encoding a novel salt stress-induced membrane protein from Rhodobacter sphaeroides f. sp. denitrificans. Appl. Microbiol. Biotechnol. 56:442-447.
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 442-447
    • Xu, X.Y.1    Kadokura, H.2    Okubo, A.3    Kitamoto, K.4    Yamakazi, S.5
  • 60
    • 77956734939 scopus 로고    scopus 로고
    • The molecular and biochemical basis of pyrophosphate-energized proton translocation at the vacuolar membrane
    • Zheng, R.-G., E. Kim, and P. A. Rea. 1997. The molecular and biochemical basis of pyrophosphate-energized proton translocation at the vacuolar membrane. Adv. Bot. Res. 25:297-337.
    • (1997) Adv. Bot. Res. , vol.25 , pp. 297-337
    • Zheng, R.-G.1    Kim, E.2    Rea, P.A.3


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