메뉴 건너뛰기




Volumn 72, Issue 4, 1997, Pages 299-315

Phosphate transport in prokaryotes: Molecules, mediators and mechanisms

Author keywords

Divalent cation; End product efflux; Phosphate chelate; Polyphosphate; Proton motive force; Transport protein

Indexed keywords

PHOSPHATE;

EID: 0030722964     PISSN: 00036072     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1000530927928     Document Type: Review
Times cited : (104)

References (198)
  • 1
    • 0018410119 scopus 로고
    • Phosphate transport in arsenate-resistant mutants of Micrococcus lysodeikticus
    • Alfasi H, Friedberg D & Friedberg I (1979) Phosphate transport in arsenate-resistant mutants of Micrococcus lysodeikticus. J. Bacteriol. 137: 69-72
    • (1979) J. Bacteriol. , vol.137 , pp. 69-72
    • Alfasi, H.1    Friedberg, D.2    Friedberg, I.3
  • 2
    • 0021719152 scopus 로고
    • Characterization of phosphate:hexose-6-phosphate antiport in membrane vesicles of Streptococcus lactis
    • Ambudkar SV & Maloney PC (1984) Characterization of phosphate:hexose-6-phosphate antiport in membrane vesicles of Streptococcus lactis. J. Biol. Chem. 259: 12576-12585
    • (1984) J. Biol. Chem. , vol.259 , pp. 12576-12585
    • Ambudkar, S.V.1    Maloney, P.C.2
  • 3
    • 0041346268 scopus 로고
    • lon-exchange systems in prokaryotes
    • Krulwhich TA (Ed) Academic Press, New York
    • Ambudkar SV & Rosen BP (1990) lon-exchange systems in prokaryotes. In: Krulwhich TA (Ed) The Bacteria, Vol XII (pp 247-271). Academic Press, New York
    • (1990) The Bacteria , vol.12 , pp. 247-271
    • Ambudkar, S.V.1    Rosen, B.P.2
  • 4
    • 0023000305 scopus 로고
    • Reconstitution of sugar phosphate transport systems of Escherichia coli
    • Ambudkar SV, Larson TJ & Maloney PC (1986a) Reconstitution of sugar phosphate transport systems of Escherichia coli. J. Biol. Chem. 261: 9083-9086
    • (1986) J. Biol. Chem. , vol.261 , pp. 9083-9086
    • Ambudkar, S.V.1    Larson, T.J.2    Maloney, P.C.3
  • 5
    • 0022467907 scopus 로고
    • Variable stoichiometry of phosphate-linked anion exchange in Streptococcus lactis: Implications for the mechanism of sugar-phosphate transport by bacteria
    • Ambudkar SV, Sonna LA & Maloney PC (1986b) Variable stoichiometry of phosphate-linked anion exchange in Streptococcus lactis: implications for the mechanism of sugar-phosphate transport by bacteria. Proc. Natl. Acad. Sci. USA 83: 280-284
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 280-284
    • Ambudkar, S.V.1    Sonna, L.A.2    Maloney, P.C.3
  • 6
    • 0022441365 scopus 로고
    • Nucleotide sequence of the phoM region of Escherichia coli: Four open reading frames may constitute an operon
    • Amemura M, Makino K, Shinagawa H & Nakata A (1986) Nucleotide sequence of the phoM region of Escherichia coli: four open reading frames may constitute an operon. J. Bacteriol. 168: 294-302
    • (1986) J. Bacteriol. , vol.168 , pp. 294-302
    • Amemura, M.1    Makino, K.2    Shinagawa, H.3    Nakata, A.4
  • 7
    • 0025029124 scopus 로고
    • Cross talk to the phosphate regulon of Escherichia coli by PhoM protein: PhoM is a histidine kinase and catalyzes phosphorylation of PhoB and PhoM-open reading frame 2
    • Amemura M, Makino K, Shinagawa H & Nakata A (1990) Cross talk to the phosphate regulon of Escherichia coli by PhoM protein: PhoM is a histidine kinase and catalyzes phosphorylation of PhoB and PhoM-open reading frame 2. J. Bacteriol. 172: 6300-6307
    • (1990) J. Bacteriol. , vol.172 , pp. 6300-6307
    • Amemura, M.1    Makino, K.2    Shinagawa, H.3    Nakata, A.4
  • 8
    • 0025033814 scopus 로고
    • Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases
    • Ames GF-L, Mimura CS&Shyamala V (1990) Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases. FEMS Microbiol. Rev. 75: 429-446
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 429-446
    • Ames, G.F.-L.1    Mimura, C.S.2    Shyamala, V.3
  • 10
    • 0021248136 scopus 로고
    • Manganese acquisition by Lactobacillus plantarum
    • Archibald FS & Duong M-N (1984) Manganese acquisition by Lactobacillus plantarum. J. Bacteriol. 158: 1-8
    • (1984) J. Bacteriol. , vol.158 , pp. 1-8
    • Archibald, F.S.1    Duong, M.-N.2
  • 11
    • 0002008370 scopus 로고
    • + transport systems in prokaryotes
    • Bakker EP (Ed) CRC Press, Boca Raton
    • + transport systems in prokaryotes. In: Bakker EP (Ed) Alkali Cation Transport Systems in Prokaryotes, (pp 205-224). CRC Press, Boca Raton
    • (1993) Alkali Cation Transport Systems in Prokaryotes , pp. 205-224
    • Bakker, E.P.1
  • 12
    • 0029744179 scopus 로고    scopus 로고
    • A phosphate transport system is required for symbiotic nitrogen fixation by Rhizobium meliloti
    • Bardin S, Dan S, Osteras M & Finan TM (1996) A phosphate transport system is required for symbiotic nitrogen fixation by Rhizobium meliloti. J. Bacteriol. 178: 4540-4547
    • (1996) J. Bacteriol. , vol.178 , pp. 4540-4547
    • Bardin, S.1    Dan, S.2    Osteras, M.3    Finan, T.M.4
  • 13
    • 0021962650 scopus 로고
    • Salmonella typhimurium contains an anion-selective outer membrane porin induced by phosphate starvation
    • Bauer K, Benz R, Brass J & Boos W (1985) Salmonella typhimurium contains an anion-selective outer membrane porin induced by phosphate starvation. J. Bacteriol. 161: 813-816
    • (1985) J. Bacteriol. , vol.161 , pp. 813-816
    • Bauer, K.1    Benz, R.2    Brass, J.3    Boos, W.4
  • 14
    • 0023802452 scopus 로고
    • The phocontrolled outer membrane porin PhoE does not contain specific binding sites for phosphate or polyphosphates
    • Bauer K, van der Ley P, Benz R & Tommassen J (1988) The phocontrolled outer membrane porin PhoE does not contain specific binding sites for phosphate or polyphosphates. J. Biol. Chem. 263: 13046-13053
    • (1988) J. Biol. Chem. , vol.263 , pp. 13046-13053
    • Bauer, K.1    Van Der Ley, P.2    Benz, R.3    Tommassen, J.4
  • 15
    • 0024424616 scopus 로고
    • One single lysine residue is responsible for the special interaction between polyphosphate and the outer membrane porin PhoE of Escherichia coli
    • Bauer K, Struyvé M, Bosch D, Benz R & Tommassen J (1989) One single lysine residue is responsible for the special interaction between polyphosphate and the outer membrane porin PhoE of Escherichia coli. J. Biol. Chem. 264: 16393-16398
    • (1989) J. Biol. Chem. , vol.264 , pp. 16393-16398
    • Bauer, K.1    Struyvé, M.2    Bosch, D.3    Benz, R.4    Tommassen, J.5
  • 16
    • 0018935067 scopus 로고
    • Isolation of Escherichia coli mutants (cpdB) deficient in periplasmic 2':3'-cyclic phosphodiesterase and genetic mapping of the cpdB locus
    • Beacham IR & Garrett S (1980) Isolation of Escherichia coli mutants (cpdB) deficient in periplasmic 2':3'-cyclic phosphodiesterase and genetic mapping of the cpdB locus. J. Gen. Microbiol. 119: 31-34
    • (1980) J. Gen. Microbiol. , vol.119 , pp. 31-34
    • Beacham, I.R.1    Garrett, S.2
  • 18
    • 0021795850 scopus 로고
    • Ion selectivity of Gramnegative bacterial porins
    • Benz R, Schmid A & Hancock REW (1985) Ion selectivity of Gramnegative bacterial porins. J. Bacteriol. 162: 722-727
    • (1985) J. Bacteriol. , vol.162 , pp. 722-727
    • Benz, R.1    Schmid, A.2    Hancock, R.E.W.3
  • 19
    • 0021104410 scopus 로고
    • The properties of citrate transport in membrane vesicles from Bacillus subtilis
    • Bergsma J & Konings WN (1983) The properties of citrate transport in membrane vesicles from Bacillus subtilis. Eur. J. Biochem. 134: 151-156
    • (1983) Eur. J. Biochem. , vol.134 , pp. 151-156
    • Bergsma, J.1    Konings, W.N.2
  • 21
    • 0009652780 scopus 로고
    • The outer membrane of Acinetobacter. structure-function relationships
    • Towner KJ, Bergogne-Bérézin E & Fewson CA (Eds) Plenum Press, New York
    • Borneleit P & Kleber H-P (1991) The outer membrane of Acinetobacter. structure-function relationships. In: Towner KJ, Bergogne-Bérézin E & Fewson CA (Eds) The Biology of Acinetobacter, (pp 259-271). Plenum Press, New York
    • (1991) The Biology of Acinetobacter , pp. 259-271
    • Borneleit, P.1    Kleber, H.-P.2
  • 22
    • 0000882208 scopus 로고
    • Hypothesis about the function of membrane-buried proline residues in transport proteins
    • Brandl CJ & Deber CM (1986) Hypothesis about the function of membrane-buried proline residues in transport proteins. Proc. Natl. Acad. Sci. USA 83: 917-921
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 917-921
    • Brandl, C.J.1    Deber, C.M.2
  • 24
    • 0025365356 scopus 로고
    • Calcium transport in bovine sperm mitochondria: Effect of substrates and phosphate. Biochim
    • Breitbart H, Wehbie R & Lardy HA (1990) Calcium transport in bovine sperm mitochondria: effect of substrates and phosphate. Biochim. Biophys. Acta 1026: 57-63
    • (1990) Biophys. Acta , vol.1026 , pp. 57-63
    • Breitbart, H.1    Wehbie, R.2    Lardy, H.A.3
  • 25
    • 0018396896 scopus 로고
    • Cation/proton antiport systems in Escherichia coli
    • Brey RN & Rosen BP (1979) Cation/proton antiport systems in Escherichia coli. J. Biol. Chem. 254: 1957-1963
    • (1979) J. Biol. Chem. , vol.254 , pp. 1957-1963
    • Brey, R.N.1    Rosen, B.P.2
  • 26
    • 0043052857 scopus 로고
    • ugp-Dependent transport system for sn-glycerol-3-phosphate of Escherichia coli
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds), American Society for Microbiology, Washington, DC
    • Brzoska P, Schweizer H, Argast M & Boos W (1987) ugp-Dependent transport system for sn-glycerol-3-phosphate of Escherichia coli. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds), Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp. 170-177). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 170-177
    • Brzoska, P.1    Schweizer, H.2    Argast, M.3    Boos, W.4
  • 27
    • 0024076898 scopus 로고
    • Characteristics of a ugp-encoded and phoB-dependent glycerophosphoryl diester phosphodiesterase which is physically dependent on the ugp transport system of Escherichia coli
    • Brzoska P & Boos W (1988) Characteristics of a ugp-encoded and phoB-dependent glycerophosphoryl diester phosphodiesterase which is physically dependent on the ugp transport system of Escherichia coli. J. Bacteriol. 170: 4125-4135
    • (1988) J. Bacteriol. , vol.170 , pp. 4125-4135
    • Brzoska, P.1    Boos, W.2
  • 28
    • 0016724271 scopus 로고
    • Phosphate transport in membrane vesicles of Paracoccus denitrificans
    • Burnell JN, John P & Whatley FR (1975) Phosphate transport in membrane vesicles of Paracoccus denitrificans. FEBS Lett. 58: 215-218
    • (1975) FEBS Lett. , vol.58 , pp. 215-218
    • Burnell, J.N.1    John, P.2    Whatley, F.R.3
  • 29
    • 0025274055 scopus 로고
    • Phosphate and calcium uptake by mitochondria and by perfused rat liver induced by the synergistic action of glucagon and vasopressin
    • Bygrave FL, Lenton L, Altin JG, Setchell BA & Karjalainen A (1990) Phosphate and calcium uptake by mitochondria and by perfused rat liver induced by the synergistic action of glucagon and vasopressin. Biochem. J. 267: 69-73
    • (1990) Biochem. J. , vol.267 , pp. 69-73
    • Bygrave, F.L.1    Lenton, L.2    Altin, J.G.3    Setchell, B.A.4    Karjalainen, A.5
  • 30
    • 0026450904 scopus 로고
    • Permeability of lipid bilayers to amino acids and phosphate
    • Chakrabarti AC & Deamer DW (1992) Permeability of lipid bilayers to amino acids and phosphate. Biochim. Biophys. Acta 1111: 171-177
    • (1992) Biochim. Biophys. Acta , vol.1111 , pp. 171-177
    • Chakrabarti, A.C.1    Deamer, D.W.2
  • 31
    • 0029967358 scopus 로고    scopus 로고
    • PstB protein of the phosphate-specific transport system of Escherichia coli is an ATPase
    • Chan F-Y & Torriani A (1996) PstB protein of the phosphate-specific transport system of Escherichia coli is an ATPase. J. Bacteriol. 178: 3974-3977
    • (1996) J. Bacteriol. , vol.178 , pp. 3974-3977
    • Chan, F.-Y.1    Torriani, A.2
  • 32
    • 0027957289 scopus 로고
    • The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein
    • Chang Z, Choudhary A, Lathigra R, Quiocho FA (1994) The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein. J. Biol. Chem. 269: 1956-1958
    • (1994) J. Biol. Chem. , vol.269 , pp. 1956-1958
    • Chang, Z.1    Choudhary, A.2    Lathigra, R.3    Quiocho, F.A.4
  • 33
    • 0014886137 scopus 로고
    • Alkaline phosphatase localization and spheroplast formation of Pseudomonas aeruginosa
    • Cheng K-J, Ingram JM & Costerton JW (1970) Alkaline phosphatase localization and spheroplast formation of Pseudomonas aeruginosa. Can. J. Microbiol. 12: 1319-1324
    • (1970) Can. J. Microbiol. , vol.12 , pp. 1319-1324
    • Cheng, K.-J.1    Ingram, J.M.2    Costerton, J.W.3
  • 35
    • 0023876711 scopus 로고
    • Arg-220 of the PstA protein is required for phosphate transport through the phosphate-specific transport system in Escherichia coli but not for alkaline phosphatase repression
    • Cox GB, Webb DC, Godovac-Zimmerman J & Rosenberg H (1988) Arg-220 of the PstA protein is required for phosphate transport through the phosphate-specific transport system in Escherichia coli but not for alkaline phosphatase repression. J. Bacteriol. 170: 2283-2286
    • (1988) J. Bacteriol. , vol.170 , pp. 2283-2286
    • Cox, G.B.1    Webb, D.C.2    Godovac-Zimmerman, J.3    Rosenberg, H.4
  • 36
    • 0024574037 scopus 로고
    • Specific amino acid residues in both the PstB and PstC proteins are required for phosphate transport by the Escherichia coli Pst system
    • Cox GB, Webb DC & Rosenberg H (1989) Specific amino acid residues in both the PstB and PstC proteins are required for phosphate transport by the Escherichia coli Pst system. J. Bacteriol. 171: 1531-1534
    • (1989) J. Bacteriol. , vol.171 , pp. 1531-1534
    • Cox, G.B.1    Webb, D.C.2    Rosenberg, H.3
  • 37
    • 0031020834 scopus 로고    scopus 로고
    • Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter
    • Dahl JL, Wei B-Y & Kadner RJ (1997) Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter. J. Biol. Chem. 272: 1910-1919
    • (1997) J. Biol. Chem. , vol.272 , pp. 1910-1919
    • Dahl, J.L.1    Wei, B.-Y.2    Kadner, R.J.3
  • 38
    • 0030874402 scopus 로고    scopus 로고
    • Proof for a nonproteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-hydroxybutanoic acid and inorganic polyphosphate
    • Das S, Lengweiler UD, Seebach D & Reusch RN (1997) Proof for a nonproteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-hydroxybutanoic acid and inorganic polyphosphate. Proc. Natl. Acad. Sci. USA 94: 9075-9079
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9075-9079
    • Das, S.1    Lengweiler, U.D.2    Seebach, D.3    Reusch, R.N.4
  • 39
    • 0020328513 scopus 로고
    • The acid phosphatase with optimum pH of 2.5 of Escherichia coli: Physiological and biochemical study
    • Dassa E, Cahu M, Desjoyaux-Cherel B & Boquet PL (1982) The acid phosphatase with optimum pH of 2.5 of Escherichia coli: Physiological and biochemical study. J. Biol. Chem. 257: 6669-6676
    • (1982) J. Biol. Chem. , vol.257 , pp. 6669-6676
    • Dassa, E.1    Cahu, M.2    Desjoyaux-Cherel, B.3    Boquet, P.L.4
  • 40
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson AL, Shuman HA & Nikaido H (1992) Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Proc. Natl. Acad. Sci. USA 89: 2360-2364
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 41
    • 0015217682 scopus 로고
    • Studies on the uptake of hexose phosphates. II. The induction of the glucose-6-phosphate transport system by exogenous but not by endogenously formed glucose-6-phosphate
    • Dietz GW & Heppel LA (1971) Studies on the uptake of hexose phosphates. II. The induction of the glucose-6-phosphate transport system by exogenous but not by endogenously formed glucose-6-phosphate. J. Biol. Chem. 246: 2885-2890
    • (1971) J. Biol. Chem. , vol.246 , pp. 2885-2890
    • Dietz, G.W.1    Heppel, L.A.2
  • 42
    • 0027458116 scopus 로고
    • ATP-dependent transport systems in bacteria and humans: Relevance to cystic fibrosis and multidrug resistance
    • Doige CA & Ames GF-L (1993) ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance. Annu. Rev. Microbiol. 47: 291-319
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 291-319
    • Doige, C.A.1    Ames, G.F.-L.2
  • 43
    • 0024198510 scopus 로고
    • A mycoplasma high-affinity transport system and the in vitro invasiveness of mouse sarcoma cells
    • Dudler R, Schmidhauser C, Parish RW, Wettenhall REH & Schmidt T (1988) A mycoplasma high-affinity transport system and the in vitro invasiveness of mouse sarcoma cells. EMBO J. 7: 3963-397
    • (1988) EMBO J. , vol.7 , pp. 3963-4397
    • Dudler, R.1    Schmidhauser, C.2    Parish, R.W.3    Wettenhall, R.E.H.4    Schmidt, T.5
  • 44
    • 0023443214 scopus 로고
    • Nucleotide sequence and transcriptional startpoint of the glpT gene of Escherichia coli: Extensive sequence homology of the G-3-P transport protein with components of the H-6-P transport system
    • Eiglmeier K, Boos W & Cole ST (1987) Nucleotide sequence and transcriptional startpoint of the glpT gene of Escherichia coli: extensive sequence homology of the G-3-P transport protein with components of the H-6-P transport system. Mol. Microbiol. 1: 251-258
    • (1987) Mol. Microbiol. , vol.1 , pp. 251-258
    • Eiglmeier, K.1    Boos, W.2    Cole, S.T.3
  • 45
    • 0021895119 scopus 로고
    • i exchange mediated by the GlpT-dependent sn-glycerol 3-phosphate transport system in Escherichia coli
    • i exchange mediated by the GlpT-dependent sn-glycerol 3-phosphate transport system in Escherichia coli. J. Bacteriol. 161: 1054-1058
    • (1985) J. Bacteriol. , vol.161 , pp. 1054-1058
    • Elvin, C.M.1    Hardy, C.M.2    Rosenberg, H.3
  • 46
    • 0022779065 scopus 로고
    • + gene product and physical mapping of the pit-gor region of the chromosome
    • + gene product and physical mapping of the pit-gor region of the chromosome. Mol. Gen. Genet. 204: 477-484
    • (1986) Mol. Gen. Genet. , vol.204 , pp. 477-484
    • Elvin, C.M.1    Dixon, N.E.2    Rosenberg, H.3
  • 47
    • 0004253329 scopus 로고
    • Molecular studies on the phosphate inorganic transport system of Escherichia coli
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) American Society for Microbiology, Washington, DC
    • Elvin CM, Hardy CM & Rosenberg H (1987) Molecular studies on the phosphate inorganic transport system of Escherichia coli. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp 156-158). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 156-158
    • Elvin, C.M.1    Hardy, C.M.2    Rosenberg, H.3
  • 48
    • 0024329881 scopus 로고
    • The biochemistry of P-glycoprotein-mediated multidrug resistence
    • Endicott JE & Ling V (1989) The biochemistry of P-glycoprotein-mediated multidrug resistence. Annu. Rev. Biochem. 58: 137-171
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 137-171
    • Endicott, J.E.1    Ling, V.2
  • 50
    • 0017576549 scopus 로고
    • Phosphate transport in Micrococcus lysodeikticus
    • Friedberg I (1977a) Phosphate transport in Micrococcus lysodeikticus. Biochim. Biophys. Acta 466: 451-460
    • (1977) Biochim. Biophys. Acta , vol.466 , pp. 451-460
    • Friedberg, I.1
  • 51
    • 0017665834 scopus 로고
    • The effect of ionophores on phosphate and arsenate transport in Micrococcus lysodeikticus
    • Friedberg I (1977b) The effect of ionophores on phosphate and arsenate transport in Micrococcus lysodeikticus. FEBS Lett. 81: 264-266
    • (1977) FEBS Lett. , vol.81 , pp. 264-266
    • Friedberg, I.1
  • 52
    • 0014081371 scopus 로고
    • Some properties of alkaline phosphatase of Pseudomonas fluorescens
    • Friedberg I & Avigad G (1967) Some properties of alkaline phosphatase of Pseudomonas fluorescens. Eur. J. Biochem. 1: 193-198
    • (1967) Eur. J. Biochem. , vol.1 , pp. 193-198
    • Friedberg, I.1    Avigad, G.2
  • 53
    • 0023388334 scopus 로고
    • Nucleotide sequence of the uhp region of Escherichia coli
    • Friedrich MJ & Kadner RJ (1987) Nucleotide sequence of the uhp region of Escherichia coli. J. Bacteriol. 169: 3556-3563
    • (1987) J. Bacteriol. , vol.169 , pp. 3556-3563
    • Friedrich, M.J.1    Kadner, R.J.2
  • 54
    • 0016218745 scopus 로고
    • The relationship between the phosphate-binding protein and a regulator gene product from Escherichia coli
    • Gerdes RG & Rosenberg H (1974) The relationship between the phosphate-binding protein and a regulator gene product from Escherichia coli. Biochim. Biophys. Acta 351: 77-86
    • (1974) Biochim. Biophys. Acta , vol.351 , pp. 77-86
    • Gerdes, R.G.1    Rosenberg, H.2
  • 55
    • 0017519497 scopus 로고
    • Restoration of phosphate transport by the phosphate-binding protein in spheroplasts of Escherichia coli
    • Gerdes RG, Strickland KP & Rosenberg H (1977) Restoration of phosphate transport by the phosphate-binding protein in spheroplasts of Escherichia coli. J. Bacteriol. 131: 512-518
    • (1977) J. Bacteriol. , vol.131 , pp. 512-518
    • Gerdes, R.G.1    Strickland, K.P.2    Rosenberg, H.3
  • 56
    • 0024198129 scopus 로고
    • Evidence for high affinity binding protein-dependent transport systems in Gram-positive bacteria and in Mycoplasma
    • Gilson E, Alloing G, Schmidt T, Claverys J-P, Dudler R & Hofnung M (1988) Evidence for high affinity binding protein-dependent transport systems in Gram-positive bacteria and in Mycoplasma. EMBO J. 7: 3971-3974
    • (1988) EMBO J. , vol.7 , pp. 3971-3974
    • Gilson, E.1    Alloing, G.2    Schmidt, T.3    Claverys, J.-P.4    Dudler, R.5    Hofnung, M.6
  • 59
    • 85021497038 scopus 로고
    • Membranes and energy transduction in bacteria
    • Harold FM (1977) Membranes and energy transduction in bacteria. Curr. Top. Bioenerg. 6: 83-149
    • (1977) Curr. Top. Bioenerg. , vol.6 , pp. 83-149
    • Harold, F.M.1
  • 61
    • 0013918182 scopus 로고
    • Interaction of arsenate with phoshate transport systems in wild-type and mutant Streptococcus faecalis
    • Harold FM & Baarda JR (1966) Interaction of arsenate with phoshate transport systems in wild-type and mutant Streptococcus faecalis. J. Bacteriol. 91: 2257-2262
    • (1966) J. Bacteriol. , vol.91 , pp. 2257-2262
    • Harold, F.M.1    Baarda, J.R.2
  • 62
    • 0014375102 scopus 로고
    • Inhibition of membrane transport in Streptococcus faecalis by uncouplers of oxidative phosphorylation and its relationship to proton conduction
    • Harold FM & Baarda JR (1968) Inhibition of membrane transport in Streptococcus faecalis by uncouplers of oxidative phosphorylation and its relationship to proton conduction. J. Bacteriol. 96: 2025-2034
    • (1968) J. Bacteriol. , vol.96 , pp. 2025-2034
    • Harold, F.M.1    Baarda, J.R.2
  • 63
    • 0016654179 scopus 로고
    • Accumulation of arsenate, phosphate, and aspartate by Streptococcus faecalis
    • Harold FM & E Spitz (1975) Accumulation of arsenate, phosphate, and aspartate by Streptococcus faecalis. J. Bacteriol. 122: 266-277
    • (1975) J. Bacteriol. , vol.122 , pp. 266-277
    • Harold, F.M.1    Spitz, E.2
  • 64
    • 0013505325 scopus 로고
    • A mutant of Streptococcus faecalis defective in phosphate transport
    • Harold FM, Harold RL & Abrams A (1965) A mutant of Streptococcus faecalis defective in phosphate transport. J. Biol. Chem. 240: 3145-3153
    • (1965) J. Biol. Chem. , vol.240 , pp. 3145-3153
    • Harold, F.M.1    Harold, R.L.2    Abrams, A.3
  • 65
    • 0001385085 scopus 로고
    • Active transport of L-α-glycerophosphate in Escherichia coli
    • Hayashi S-I, Koch JP & Lin ECC (1964) Active transport of L-α-glycerophosphate in Escherichia coli. J. Biol. Chem. 239: 3098-3105
    • (1964) J. Biol. Chem. , vol.239 , pp. 3098-3105
    • Hayashi, S.-I.1    Koch, J.P.2    Lin, E.C.C.3
  • 67
    • 0026399707 scopus 로고
    • Studies of translocation catalysis
    • Henderson PJF (1991) Studies of translocation catalysis. Bioscience Reports 11: 477-538
    • (1991) Bioscience Reports , vol.11 , pp. 477-538
    • Henderson, P.J.F.1
  • 68
    • 0021101144 scopus 로고
    • Maltose and lactose transport in Escherichia coli. Examples of two different types of concentrative transport system
    • Hengge R & Boos W (1983) Maltose and lactose transport in Escherichia coli. Examples of two different types of concentrative transport system. Biochim. Biophys. Acta 737: 443-478
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 443-478
    • Hengge, R.1    Boos, W.2
  • 69
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins CF (1992) ABC transporters: from microorganisms to man. Annu. Rev. Cell. Biol. 8: 67-113
    • (1992) Annu. Rev. Cell. Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 71
    • 0029976302 scopus 로고    scopus 로고
    • The signal-transduction network for Pho regulation in Bacillus subtilis
    • Hulett FM (1996) The signal-transduction network for Pho regulation in Bacillus subtilis. Mol. Microbiol. 19: 933-939
    • (1996) Mol. Microbiol. , vol.19 , pp. 933-939
    • Hulett, F.M.1
  • 72
    • 0039289443 scopus 로고
    • Alkaline phosphatase from Bacillus licheniformis: Proteins and genes
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) American Society for Microbiology, Washington, DC
    • Hulett FM (1987) Alkaline phosphatase from Bacillus licheniformis: proteins and genes. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp. 43-48). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 43-48
    • Hulett, F.M.1
  • 73
    • 0027214685 scopus 로고
    • Interplay between the membrane-associated UhpB and UhpC regulatory proteins
    • Island MD & Kadner RJ (1993) Interplay between the membrane-associated UhpB and UhpC regulatory proteins. J. Bacteriol. 175: 5028-5034
    • (1993) J. Bacteriol. , vol.175 , pp. 5028-5034
    • Island, M.D.1    Kadner, R.J.2
  • 74
    • 0026643236 scopus 로고
    • Structure and function of the uhp genes for the sugar phosphate transport system in Escherichia coli and Salmonella typhimurium
    • Island MD, Wei B-Y & Kadner RJ (1992) Structure and function of the uhp genes for the sugar phosphate transport system in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 174: 2754-2762
    • (1992) J. Bacteriol. , vol.174 , pp. 2754-2762
    • Island, M.D.1    Wei, B.-Y.2    Kadner, R.J.3
  • 75
    • 9044252427 scopus 로고
    • Active transport: Membrane vesicles, bioenergetics, molecules and mechanisms
    • Krulwhich TA (Ed) Academic Press, New York
    • Kaback HR (1990) Active transport: membrane vesicles, bioenergetics, molecules and mechanisms. In: Krulwhich TA (Ed) The Bacteria, Vol. XII (pp 151-202). Academic Press, New York
    • (1990) The Bacteria , vol.12 , pp. 151-202
    • Kaback, H.R.1
  • 76
    • 0026744648 scopus 로고
    • Two mechanisms for growth inhibition by elevated transport of sugar phosphates in Escherichia coli
    • Kadner RJ, Murphy GP & Stephens GM (1992) Two mechanisms for growth inhibition by elevated transport of sugar phosphates in Escherichia coli. J. Gen. Microbiol. 138: 2007-2014
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2007-2014
    • Kadner, R.J.1    Murphy, G.P.2    Stephens, G.M.3
  • 77
    • 0025966270 scopus 로고
    • Dual regulation of the ugp operon by phosphate and carbon starvation at two interspaced promoters
    • Kasahara M, Makino K, Amemura M, Nakata A & Shinagawa H (1991) Dual regulation of the ugp operon by phosphate and carbon starvation at two interspaced promoters. J. Bacteriol. 173: 549-558
    • (1991) J. Bacteriol. , vol.173 , pp. 549-558
    • Kasahara, M.1    Makino, K.2    Amemura, M.3    Nakata, A.4    Shinagawa, H.5
  • 78
    • 0019832978 scopus 로고
    • 4 dicarboxylate transport in Bacillus subtilis
    • 4 dicarboxylate transport in Bacillus subtilis. Can. J. Microbiol. 27: 1194-1201
    • (1981) Can. J. Microbiol. , vol.27 , pp. 1194-1201
    • Kay, W.W.1    Ghei, O.K.2
  • 79
    • 0029844678 scopus 로고    scopus 로고
    • Involvement of the sensor kinase EnvZ in the in vivo activation of the response-regulator PhoB by acetyl phosphate
    • Kim S-K, Wilmes-Riesenberg MR & Wanner BL (1996) Involvement of the sensor kinase EnvZ in the in vivo activation of the response-regulator PhoB by acetyl phosphate. Mol. Microbiol. 22: 2534-2539
    • (1996) Mol. Microbiol. , vol.22 , pp. 2534-2539
    • Kim, S.-K.1    Wilmes-Riesenberg, M.R.2    Wanner, B.L.3
  • 80
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function and biogenesis
    • Klionsky DJ, Herman PK & Emr SD (1990) The fungal vacuole: composition, function and biogenesis. Microbiol. Rev. 54: 266-292
    • (1990) Microbiol. Rev. , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 81
    • 0017891569 scopus 로고
    • Phosphate transport in membrane vesicles from Escherichia coli
    • Konings WN & Rosenberg H (1978) Phosphate transport in membrane vesicles from Escherichia coli. Biochim. Biophys. Acta 508: 370-378
    • (1978) Biochim. Biophys. Acta , vol.508 , pp. 370-378
    • Konings, W.N.1    Rosenberg, H.2
  • 83
    • 0020403106 scopus 로고
    • PhoE protein pore of the outer membrane of Escherichia coli K-12 is a particularly efficient channel for organic and inorganic phosphate
    • Korteland J, Tommassen J& Lugtenberg B (1982) PhoE protein pore of the outer membrane of Escherichia coli K-12 is a particularly efficient channel for organic and inorganic phosphate. Biochim. Biophys. Acta 690: 282-289
    • (1982) Biochim. Biophys. Acta , vol.690 , pp. 282-289
    • Korteland, J.1    Tommassen, J.2    Lugtenberg, B.3
  • 86
    • 0023001016 scopus 로고
    • Crystallization and X-ray diffraction studies of a phosphate-binding protein involved in active transport in Escherichia coli
    • Kubena BD, Luecke H, Rosenberg H & Quiocho FA (1986) Crystallization and X-ray diffraction studies of a phosphate-binding protein involved in active transport in Escherichia coli. J. Biol. Chem. 261: 7995-7996
    • (1986) J. Biol. Chem. , vol.261 , pp. 7995-7996
    • Kubena, B.D.1    Luecke, H.2    Rosenberg, H.3    Quiocho, F.A.4
  • 87
    • 0019782008 scopus 로고
    • Transport of inorganic phosphate in Pseudomonas aeruginosa
    • Lacoste A-M, Cassaigne A & Neuzil E (1981) Transport of inorganic phosphate in Pseudomonas aeruginosa. Curr. Microbiol. 6: 115-120
    • (1981) Curr. Microbiol. , vol.6 , pp. 115-120
    • Lacoste, A.-M.1    Cassaigne, A.2    Neuzil, E.3
  • 88
    • 9844259117 scopus 로고
    • glpT-Dependent transport of sn-glycerol-3-phosphate in Escherichia coli K-12
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A and Yagil E (Eds) American Society for Microbiology, Washington, DC
    • Larson TJ (1987) glpT-Dependent transport of sn-glycerol-3-phosphate in Escherichia coli K-12. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A and Yagil E (Eds) Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp 164-169). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 164-169
    • Larson, T.J.1
  • 89
    • 0020641705 scopus 로고
    • Periplasmic glycerophospodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon
    • Larson TJ, Ehrmann M & Boos W (1983) Periplasmic glycerophospodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon. J. Biol. Chem. 258: 5428-5432
    • (1983) J. Biol. Chem. , vol.258 , pp. 5428-5432
    • Larson, T.J.1    Ehrmann, M.2    Boos, W.3
  • 90
    • 9844259117 scopus 로고
    • glpT-Dependent transport of sn-glycerol-3-phosphate in Escherichia coli K-12
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) American Society for Microbiology, Washington, DC
    • Larson TJ (1987) glpT-Dependent transport of sn-glycerol-3-phosphate in Escherichia coli K-12. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp 164-169). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 164-169
    • Larson, T.J.1
  • 91
    • 0019333907 scopus 로고
    • Glucose-6-phosphate transport in membrane vesicles isolated from Escherichia coli: Effect of imposed electrical potential and pH gradient
    • Leblanc G, Rimon G & Kaback HR (1980) Glucose-6-phosphate transport in membrane vesicles isolated from Escherichia coli: Effect of imposed electrical potential and pH gradient. Biochemistry 19: 2522-2528
    • (1980) Biochemistry , vol.19 , pp. 2522-2528
    • Leblanc, G.1    Rimon, G.2    Kaback, H.R.3
  • 92
    • 0024358062 scopus 로고
    • Phosphate regulon in members of the family Enterobacteriaceae: Comparison of the phoB-phoR operons of Escherichia coli, Shigella dysenteriae, andKlebsiella pneumoniae
    • Lee T-Y, Makino K, Shinagawa H, Amemura M & Nakata A (1989) Phosphate regulon in members of the family Enterobacteriaceae: comparison of the phoB-phoR operons of Escherichia coli, Shigella dysenteriae, andKlebsiella pneumoniae. J. Bacteriol. 171: 6593-6599
    • (1989) J. Bacteriol. , vol.171 , pp. 6593-6599
    • Lee, T.-Y.1    Makino, K.2    Shinagawa, H.3    Amemura, M.4    Nakata, A.5
  • 93
    • 8244238391 scopus 로고    scopus 로고
    • Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG
    • Lefèvre P, Braibant M, de Wit L, Kalai M, Röeper D, Grötzinger J, Delville J-P, Peirs P, Ooms J, Huygen K & Content J (1997) Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG. J. Bacteriol. 179: 2900-2906
    • (1997) J. Bacteriol. , vol.179 , pp. 2900-2906
    • Lefèvre, P.1    Braibant, M.2    De Wit, L.3    Kalai, M.4    Röeper, D.5    Grötzinger, J.6    Delville, J.-P.7    Peirs, P.8    Ooms, J.9    Huygen, K.10    Content, J.11
  • 94
    • 0014841199 scopus 로고
    • Mitochondria and calcium transport
    • Lehninger AL (1970) Mitochondria and calcium transport. Biochem. J. 119: 129-138
    • (1970) Biochem. J. , vol.119 , pp. 129-138
    • Lehninger, A.L.1
  • 95
    • 0025356011 scopus 로고
    • Topology of the Escherichia coli UhpT sugar-phosphate transporter analyzed using TnphoA fusions
    • Lloyd AD & Kadner RJ (1990) Topology of the Escherichia coli UhpT sugar-phosphate transporter analyzed using TnphoA fusions. J. Bacteriol. 172: 1688-1693
    • (1990) J. Bacteriol. , vol.172 , pp. 1688-1693
    • Lloyd, A.D.1    Kadner, R.J.2
  • 96
    • 0025000575 scopus 로고
    • High specificity of a phosphate transport protein determined by hydrogen bonds
    • Luecke H & Quiocho FA (1990) High specificity of a phosphate transport protein determined by hydrogen bonds. Nature 347: 402-406
    • (1990) Nature , vol.347 , pp. 402-406
    • Luecke, H.1    Quiocho, F.A.2
  • 97
    • 0020636951 scopus 로고
    • Molecular architecture and functioning of the outer membrane of Escherichia coli and other Gram-negative bacteria
    • Lugtenberg B & van Alphen L (1983) Molecular architecture and functioning of the outer membrane of Escherichia coli and other Gram-negative bacteria. Biochim. Biophys. Acta 737: 51-115
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 51-115
    • Lugtenberg, B.1    Van Alphen, L.2
  • 98
    • 0009573805 scopus 로고
    • Calcium transport in prokaryotes
    • Rosen BP & Silver S (Eds) Academic Press, New York
    • Lynn AR & Rosen BP (1987) Calcium transport in prokaryotes. In: Rosen BP & Silver S (Eds) Ion Transport in Prokaryotes, (pp 181-201). Academic Press, New York
    • (1987) Ion Transport in Prokaryotes , pp. 181-201
    • Lynn, A.R.1    Rosen, B.P.2
  • 100
    • 0022977821 scopus 로고
    • Nucleotide sequence of the phoR gene, a regulatory gene of the phosphate regulon of Escherichia coli
    • Makino K, Shinagawa H, Amemura M & Nakata A (1986a) Nucleotide sequence of the phoR gene, a regulatory gene of the phosphate regulon of Escherichia coli. J. Mol. Biol. 192: 549-556
    • (1986) J. Mol. Biol. , vol.192 , pp. 549-556
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Nakata, A.4
  • 101
    • 0022533109 scopus 로고
    • Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli
    • Makino K, Shinagawa H, Amemura M & Nakata A (1986b) Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli. J. Mol. Biol. 190: 37-44
    • (1986) J. Mol. Biol. , vol.190 , pp. 37-44
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Nakata, A.4
  • 102
    • 0023801563 scopus 로고
    • Regulation of the phosphate regulon of Escherichia coli. Activation of pstS transcription by phoB protein in vitro
    • Makino K, Shinagawa H, Amemura M, Kimura S, Nakata A & Ishihama A (1988) Regulation of the phosphate regulon of Escherichia coli. Activation of pstS transcription by phoB protein in vitro. J. Mol. Biol. 203: 85-95
    • (1988) J. Mol. Biol. , vol.203 , pp. 85-95
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kimura, S.4    Nakata, A.5    Ishihama, A.6
  • 103
    • 0024811077 scopus 로고
    • Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins
    • Makino K, Shinagawa H, Amemura M, Kawamoto T, Yamada M & Nakata A (1989) Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins. J. Mol. Biol. 210: 551-559
    • (1989) J. Mol. Biol. , vol.210 , pp. 551-559
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kawamoto, T.4    Yamada, M.5    Nakata, A.6
  • 104
    • 0021266951 scopus 로고
    • Phosphate:hexose-6-phosphate antiport in Streptococcus lactis
    • Maloney PC, Ambudkar SV, Thomas J & Schiller L (1984) Phosphate:hexose-6-phosphate antiport in Streptococcus lactis. J. Bacteriol. 158: 238-245
    • (1984) J. Bacteriol. , vol.158 , pp. 238-245
    • Maloney, P.C.1    Ambudkar, S.V.2    Thomas, J.3    Schiller, L.4
  • 105
    • 4243208291 scopus 로고
    • Anion exchange as the molecular basis of sugar phosphate transport by bacteria
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) American Society for Microbiology, Washington, DC
    • Maloney PC, Ambudkar SV & Sonna LA (1987) Anion exchange as the molecular basis of sugar phosphate transport by bacteria. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp 191-196). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 191-196
    • Maloney, P.C.1    Ambudkar, S.V.2    Sonna, L.A.3
  • 107
    • 0027507306 scopus 로고
    • A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport
    • Marger M & Saier MH (1993) A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport. Trends Biochem. Sci. 18: 13-20
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 13-20
    • Marger, M.1    Saier, M.H.2
  • 108
    • 0029768915 scopus 로고    scopus 로고
    • Enzymatic and biochemical probes of residues external to the translocation pathway of UhpT, the sugar phosphate carrier of Escherichia coli
    • Matos M, Fann M-C, Yan R-T & Maloney PC (1996) Enzymatic and biochemical probes of residues external to the translocation pathway of UhpT, the sugar phosphate carrier of Escherichia coli. J. Biol. Chem. 271: 18571-18575
    • (1996) J. Biol. Chem. , vol.271 , pp. 18571-18575
    • Matos, M.1    Fann, M.-C.2    Yan, R.-T.3    Maloney, P.C.4
  • 109
    • 0027207516 scopus 로고
    • Is acetyl phosphate a global signal in Escherichia coli?
    • McCleary WR, Stock JB & Ninfa AJ (1993) Is acetyl phosphate a global signal in Escherichia coli? J. Bacteriol. 175: 2793-2798
    • (1993) J. Bacteriol. , vol.175 , pp. 2793-2798
    • McCleary, W.R.1    Stock, J.B.2    Ninfa, A.J.3
  • 110
    • 0014683612 scopus 로고
    • The binding and release of phosphate by a protein isolated from Escherichia coli
    • Medveczky N & Rosenberg H (1969) The binding and release of phosphate by a protein isolated from Escherichia coli. Biochim. Biophys. Acta 192: 369-371
    • (1969) Biochim. Biophys. Acta , vol.192 , pp. 369-371
    • Medveczky, N.1    Rosenberg, H.2
  • 111
    • 0009006057 scopus 로고
    • The phosphate-binding protein of Escherichia coli
    • Medveczky N & Rosenberg H (1970) The phosphate-binding protein of Escherichia coli. Biochim. Biophys. Acta 211: 158-168
    • (1970) Biochim. Biophys. Acta , vol.211 , pp. 158-168
    • Medveczky, N.1    Rosenberg, H.2
  • 112
  • 113
    • 0015505517 scopus 로고
    • Effect of cations and protons on the kinetics of substrate uptake in rat liver mitochondria
    • Meisner H, Palmieri F & Quagliariello E (1972) Effect of cations and protons on the kinetics of substrate uptake in rat liver mitochondria. Biochemistry 11: 949-955
    • (1972) Biochemistry , vol.11 , pp. 949-955
    • Meisner, H.1    Palmieri, F.2    Quagliariello, E.3
  • 114
    • 0026770519 scopus 로고
    • Promoter elements required for positive control of transcription of the Escherichia coli uhpT gene
    • Merkel TJ, Nelson DM, Brauer CL & Kadner RJ (1992) Promoter elements required for positive control of transcription of the Escherichia coli uhpT gene. J. Bacteriol. 174: 2763-2770
    • (1992) J. Bacteriol. , vol.174 , pp. 2763-2770
    • Merkel, T.J.1    Nelson, D.M.2    Brauer, C.L.3    Kadner, R.J.4
  • 116
    • 0007896105 scopus 로고
    • Transport of phosphate across the osmotic barrier of Micrococcus pyogenes: Specificity and kinetics
    • Mitchell P (1954) Transport of phosphate across the osmotic barrier of Micrococcus pyogenes: specificity and kinetics. J. Gen. Microbiol. 11: 73-82
    • (1954) J. Gen. Microbiol. , vol.11 , pp. 73-82
    • Mitchell, P.1
  • 117
    • 0026620296 scopus 로고
    • Role of PhoU in phosphate transport and alkaline phosphatase regulation
    • Muda M, Rao NN & Torriani A (1992) Role of PhoU in phosphate transport and alkaline phosphatase regulation. J. Bacteriol. 174: 8057-8064
    • (1992) J. Bacteriol. , vol.174 , pp. 8057-8064
    • Muda, M.1    Rao, N.N.2    Torriani, A.3
  • 118
    • 0021231260 scopus 로고
    • Regulation of the phosphate regulon in Escherichia coli K-12: Regulation of the negative regulatory gene phoU and identification of the gene product
    • Nakata A, Amemura M & Shinagawa H (1984) Regulation of the phosphate regulon in Escherichia coli K-12: regulation of the negative regulatory gene phoU and identification of the gene product. J. Bacteriol. 159: 979-985
    • (1984) J. Bacteriol. , vol.159 , pp. 979-985
    • Nakata, A.1    Amemura, M.2    Shinagawa, H.3
  • 119
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu HC & Heppel LA (1965) The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240: 3685-3692
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 121
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H & Vaara M (1985) Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49: 1-32
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 122
    • 0029947312 scopus 로고    scopus 로고
    • Molecular analysis of the phosphate-specific transport (pst) operon of Pseudomonas aeruginosa
    • Nikata T, Sakai Y, Shibata K, Kato K, Kuroda A & Ohtake H (1996) Molecular analysis of the phosphate-specific transport (pst) operon of Pseudomonas aeruginosa. Mol. Gen. Genet. 250: 692-698
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 692-698
    • Nikata, T.1    Sakai, Y.2    Shibata, K.3    Kato, K.4    Kuroda, A.5    Ohtake, H.6
  • 123
    • 0027171026 scopus 로고
    • Leucine/isoleucine/valine-binding protein contracts upon binding of ligand
    • Olah GA, Trakhanov S, Trewhella J & Quiocho FA (1993) Leucine/isoleucine/valine-binding protein contracts upon binding of ligand. J. Biol. Chem. 268: 16241-16247
    • (1993) J. Biol. Chem. , vol.268 , pp. 16241-16247
    • Olah, G.A.1    Trakhanov, S.2    Trewhella, J.3    Quiocho, F.A.4
  • 124
    • 0018828451 scopus 로고
    • Expression of outer membrane protein of Escherichia coli K-12 by phosphate limitation
    • Overbeeke N & Lugtenberg B (1980) Expression of outer membrane protein of Escherichia coli K-12 by phosphate limitation. FEBS Lett. 112: 229-232
    • (1980) FEBS Lett. , vol.112 , pp. 229-232
    • Overbeeke, N.1    Lugtenberg, B.2
  • 125
    • 0024120551 scopus 로고
    • Nucleotide sequence of the ugp genes of Escherichia coli K-12: Homology to the maltose system
    • Overduin P, Boos W & Tommassen J (1988) Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to the maltose system. Mol. Microbiol. 2: 767-775
    • (1988) Mol. Microbiol. , vol.2 , pp. 767-775
    • Overduin, P.1    Boos, W.2    Tommassen, J.3
  • 126
    • 0026031219 scopus 로고
    • The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation
    • Perego M, Higgins CF, Pearce SR, Gallagher MP & Hoch JA (1991) The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation. Mol. Microbiol. 5: 173-185
    • (1991) Mol. Microbiol. , vol.5 , pp. 173-185
    • Perego, M.1    Higgins, C.F.2    Pearce, S.R.3    Gallagher, M.P.4    Hoch, J.A.5
  • 127
    • 0014028936 scopus 로고
    • Induction of an active transport system of glucose-6-phosphate in Escherichia coli
    • Pogell BM, Maity BR, Frumkin S & Shapiro S (1966) Induction of an active transport system of glucose-6-phosphate in Escherichia coli. Arch. Biochem. Biophys. 116: 406-415
    • (1966) Arch. Biochem. Biophys. , vol.116 , pp. 406-415
    • Pogell, B.M.1    Maity, B.R.2    Frumkin, S.3    Shapiro, S.4
  • 128
    • 0021753892 scopus 로고
    • Phosphate transport in Pseudomonas aeruginosa. Involvement of a periplasmic phosphate-binding protein
    • Poole K & Hancock REW (1984) Phosphate transport in Pseudomonas aeruginosa. Involvement of a periplasmic phosphate-binding protein. Eur. J. Biochem. 144: 607-612
    • (1984) Eur. J. Biochem. , vol.144 , pp. 607-612
    • Poole, K.1    Hancock, R.E.W.2
  • 129
    • 0022515695 scopus 로고
    • Phosphate-starvation-induced outer membrane proteins of members of the families Enterobacteri-aceae and Pseudomonodaceae: Demonstration of immunological cross-reactivity with an antiserum specific for porin protein P of Pseudomonas aeruginosa
    • Poole K & Hancock REW (1986) Phosphate-starvation-induced outer membrane proteins of members of the families Enterobacteri-aceae and Pseudomonodaceae: demonstration of immunological cross-reactivity with an antiserum specific for porin protein P of Pseudomonas aeruginosa. J. Bacteriol. 165: 987-993
    • (1986) J. Bacteriol. , vol.165 , pp. 987-993
    • Poole, K.1    Hancock, R.E.W.2
  • 130
    • 0023589202 scopus 로고
    • Dependence of Streptococcus lactis phosphate transport on internal phosphate concentration and internal pH
    • Poolman B, Nijssen RMJ & Konings WN (1987) Dependence of Streptococcus lactis phosphate transport on internal phosphate concentration and internal pH. J. Bacteriol. 169: 5373-5378
    • (1987) J. Bacteriol. , vol.169 , pp. 5373-5378
    • Poolman, B.1    Nijssen, R.M.J.2    Konings, W.N.3
  • 131
    • 9844269771 scopus 로고
    • Energy-linked transport in mitochondria
    • Racker E (Ed) Van Nostrand-Reinhold, New York
    • Pressman BC (1970) Energy-linked transport in mitochondria. In: Racker E (Ed) Membranes of Mitochondria and Chloroplasts, (pp 213-250). Van Nostrand-Reinhold, New York
    • (1970) Membranes of Mitochondria and Chloroplasts , pp. 213-250
    • Pressman, B.C.1
  • 132
    • 0024604620 scopus 로고
    • Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex
    • Prossnitz E, Gee A & Ames GF-L (1989) Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex. J. Biol. Chem. 264: 5006-5014
    • (1989) J. Biol. Chem. , vol.264 , pp. 5006-5014
    • Prossnitz, E.1    Gee, A.2    Ames, G.F.-L.3
  • 133
    • 0030895003 scopus 로고    scopus 로고
    • The psf operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the Pho regulon
    • Qi Y, Kobayashi Y & Hulett FM (1997) The psf operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the Pho regulon. J. Bacteriol. 179: 2534-2539
    • (1997) J. Bacteriol. , vol.179 , pp. 2534-2539
    • Qi, Y.1    Kobayashi, Y.2    Hulett, F.M.3
  • 134
    • 0017117692 scopus 로고
    • Studies on phosphate transport in Escherichia coli. I. Reexamination of the effect of osmotic and cold shock on phosphate uptake and some attempts to restore uptake with phosphate binding protein
    • Rae AS & Strickland KP (1976a) Studies on phosphate transport in Escherichia coli. I. Reexamination of the effect of osmotic and cold shock on phosphate uptake and some attempts to restore uptake with phosphate binding protein. Biochim. Biophys. Acta 433: 555-563
    • (1976) Biochim. Biophys. Acta , vol.433 , pp. 555-563
    • Rae, A.S.1    Strickland, K.P.2
  • 135
    • 0017198184 scopus 로고
    • Studies on phosphate transport in Escherichia coli. II. Effects of metabolic inhibitors and divalent cations
    • Rae AS & Strickland KP (1976b) Studies on phosphate transport in Escherichia coli. II. Effects of metabolic inhibitors and divalent cations. Biochim. Biophys. Acta 433: 564-582
    • (1976) Biochim. Biophys. Acta , vol.433 , pp. 564-582
    • Rae, A.S.1    Strickland, K.P.2
  • 136
    • 0029911577 scopus 로고    scopus 로고
    • Inorganic polyphosphate supports resistance and survival of stationary-phase Escherichia coli
    • Rao NN & Kornberg A (1996) Inorganic polyphosphate supports resistance and survival of stationary-phase Escherichia coli. J. Bacteriol. 178: 1394-1400
    • (1996) J. Bacteriol. , vol.178 , pp. 1394-1400
    • Rao, N.N.1    Kornberg, A.2
  • 137
    • 0027507211 scopus 로고
    • Effect of glpT and glpD mutations on expression of the phoA gene in Escherichia coli
    • Rao NN, Roberts MF, Torriani A & Yashphe Y (1993) Effect of glpT and glpD mutations on expression of the phoA gene in Escherichia coli. J. Bacteriol. 175: 74-79
    • (1993) J. Bacteriol. , vol.175 , pp. 74-79
    • Rao, N.N.1    Roberts, M.F.2    Torriani, A.3    Yashphe, Y.4
  • 138
    • 0023120321 scopus 로고
    • Mechanism and regulation of phosphate transport in Streptococcus pyogenes
    • Reizer J & Saier MH (1987) Mechanism and regulation of phosphate transport in Streptococcus pyogenes. J. Bacteriol. 169: 297-302
    • (1987) J. Bacteriol. , vol.169 , pp. 297-302
    • Reizer, J.1    Saier, M.H.2
  • 139
    • 0025962494 scopus 로고
    • High biological nutrient removal from domestic waste water in combination with phosphorus recycling
    • Rensink JH, Eggers E & Donkers HJGW (1991) High biological nutrient removal from domestic waste water in combination with phosphorus recycling. Water Sci. Technol. 23: 651-657
    • (1991) Water Sci. Technol. , vol.23 , pp. 651-657
    • Rensink, J.H.1    Eggers, E.2    Donkers, H.J.G.W.3
  • 140
  • 142
    • 0039596658 scopus 로고
    • Phosphate transport in prokaryotes
    • Rosen BP & Silver S (Eds) Academic Press, New York
    • Rosenberg H (1987) Phosphate transport in prokaryotes. In: Rosen BP & Silver S (Eds) Ion Transport in Prokaryotes, (pp 205-248). Academic Press, New York
    • (1987) Ion Transport in Prokaryotes , pp. 205-248
    • Rosenberg, H.1
  • 143
    • 0014410574 scopus 로고
    • The isolation of a mutant of Bacillus cereus deficient in phosphate uptake
    • Rosenberg H & La Nauze JM (1968) The isolation of a mutant of Bacillus cereus deficient in phosphate uptake. Biochim. Biophys. Acta 156: 381-388
    • (1968) Biochim. Biophys. Acta , vol.156 , pp. 381-388
    • Rosenberg, H.1    La Nauze, J.M.2
  • 145
    • 0017521785 scopus 로고
    • Two systems for the uptake of phosphate in Escherichia coli
    • Rosenberg H, Gerdes RG & Chegwidden K (1977) Two systems for the uptake of phosphate in Escherichia coli. J. Bacteriol. 131: 505-511
    • (1977) J. Bacteriol. , vol.131 , pp. 505-511
    • Rosenberg, H.1    Gerdes, R.G.2    Chegwidden, K.3
  • 146
    • 0018387840 scopus 로고
    • Energy coupling to the transport of inorganic phosphate in Escherichia coli K-12
    • Rosenberg H, Gerdes RG & Harold FM (1979) Energy coupling to the transport of inorganic phosphate in Escherichia coli K-12. Biochem. J. 178: 133-137
    • (1979) Biochem. J. , vol.178 , pp. 133-137
    • Rosenberg, H.1    Gerdes, R.G.2    Harold, F.M.3
  • 147
    • 85022509471 scopus 로고
    • Energy coupling to phosphate transport in Escherichia coli
    • Leive L & Schlessinger D (Eds) American Society for Microbiology, Washington, DC
    • Rosenberg H, Hardy CM & Surin BP (1984) Energy coupling to phosphate transport in Escherichia coli. In: Leive L & Schlessinger D (Eds) Microbiology, (pp 50-52). American Society for Microbiology, Washington, DC
    • (1984) Microbiology , pp. 50-52
    • Rosenberg, H.1    Hardy, C.M.2    Surin, B.P.3
  • 148
    • 0018733366 scopus 로고
    • Linked transport of phosphate, potassium ions and protons in Escherichia coli
    • Russell LM & Rosenberg H (1979) Linked transport of phosphate, potassium ions and protons in Escherichia coli. Biochem. J. 184: 13-21
    • (1979) Biochem. J. , vol.184 , pp. 13-21
    • Russell, L.M.1    Rosenberg, H.2
  • 149
    • 0019325467 scopus 로고
    • The nature of the link between potassium transport and phosphate transport in Escherichia coli
    • Russell LM & Rosenberg H (1980) The nature of the link between potassium transport and phosphate transport in Escherichia coli. Biochem. J. 188: 715-723
    • (1980) Biochem. J. , vol.188 , pp. 715-723
    • Russell, L.M.1    Rosenberg, H.2
  • 150
    • 0026549141 scopus 로고
    • Gene regulation of plasmidand chromosome-determined inorganic ion transport in bacteria
    • Silver S & Walderhaug M (1992) Gene regulation of plasmidand chromosome-determined inorganic ion transport in bacteria. Microbiol. Rev. 56: 195-228
    • (1992) Microbiol. Rev. , vol.56 , pp. 195-228
    • Silver, S.1    Walderhaug, M.2
  • 152
    • 0028986943 scopus 로고
    • 2+ transport system in Gram-negative bacteria
    • 2+ transport system in Gram-negative bacteria. J. Bacteriol. 177: 1638-1640
    • (1995) J. Bacteriol. , vol.177 , pp. 1638-1640
    • Smith, R.L.1    Maguire, M.E.2
  • 153
    • 0027193293 scopus 로고
    • Sequence and topology of the CorA magnesium transport systems of Salmonella typhimurium and Escherichia coli: Identification of a new class of transport protein
    • Smith RL, Banks JL, Snavely MD & Maguire ME (1993) Sequence and topology of the CorA magnesium transport systems of Salmonella typhimurium and Escherichia coli: identification of a new class of transport protein. J. Biol. Chem. 268: 14071-14080.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14071-14080
    • Smith, R.L.1    Banks, J.L.2    Snavely, M.D.3    Maguire, M.E.4
  • 155
    • 0023888859 scopus 로고
    • Identification and functional reconstitution of phosphate:sugar-phosphate antiport in Staphylococcus aureus
    • Sonna LA & Maloney PC (1988) Identification and functional reconstitution of phosphate:sugar-phosphate antiport in Staphylococcus aureus. J. Membr. Biol. 101: 267-274
    • (1988) J. Membr. Biol. , vol.101 , pp. 267-274
    • Sonna, L.A.1    Maloney, P.C.2
  • 156
    • 0023890555 scopus 로고
    • The mechanism of glucose 6-phosphate transport by Escherichia coli
    • Sonna LA, Ambudkar SV & Maloney PC (1988) The mechanism of glucose 6-phosphate transport by Escherichia coli. J. Biol. Chem. 263: 6625-6630
    • (1988) J. Biol. Chem. , vol.263 , pp. 6625-6630
    • Sonna, L.A.1    Ambudkar, S.V.2    Maloney, P.C.3
  • 157
    • 0027441190 scopus 로고
    • Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: Evidence of a new role for the PhoU protein in the phosphate regulon
    • Steed PM & Wanner BL (1993) Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon. J. Bacteriol. 175: 6797-6809
    • (1993) J. Bacteriol. , vol.175 , pp. 6797-6809
    • Steed, P.M.1    Wanner, B.L.2
  • 158
    • 0021185739 scopus 로고
    • Influence of nutrient limitation and growth rate on the outer membrane proteins of Klebsiella aerogenes NCTC 418
    • Sterkenburg A, Vlegels E & Wouters JTM (1984) Influence of nutrient limitation and growth rate on the outer membrane proteins of Klebsiella aerogenes NCTC 418. J. Gen. Microbiol. 130: 2347-2355
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2347-2355
    • Sterkenburg, A.1    Vlegels, E.2    Wouters, J.T.M.3
  • 159
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock JB, Ninfa AJ & Stock AM (1989) Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 53: 450-490
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 160
    • 0021320086 scopus 로고
    • Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: Complete nucleotide sequence of the phoS gene
    • Surin BP, Jans DA, Fimmel AL, Shaw DC, Cox GB & Rosenberg H (1984) Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene. J. Bacteriol. 157: 772-778
    • (1984) J. Bacteriol. , vol.157 , pp. 772-778
    • Surin, B.P.1    Jans, D.A.2    Fimmel, A.L.3    Shaw, D.C.4    Cox, G.B.5    Rosenberg, H.6
  • 161
    • 0021927285 scopus 로고
    • Phosphate-specific transport system of Escherichia coli: Nucleotide sequence and gene-polypeptide relationships
    • Surin BP, Rosenberg H & Cox GB (1985) Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships. J. Bacteriol. 161: 189-198
    • (1985) J. Bacteriol. , vol.161 , pp. 189-198
    • Surin, B.P.1    Rosenberg, H.2    Cox, G.B.3
  • 162
    • 0004253329 scopus 로고
    • Molecular studies on the phosphate-specific transport system of Escherichia coli
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) American Society for Microbiology, Washington, DC
    • Surin BP, Cox GB & Rosenberg H (1987) Molecular studies on the phosphate-specific transport system of Escherichia coli. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp 145-149). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 145-149
    • Surin, B.P.1    Cox, G.B.2    Rosenberg, H.3
  • 163
    • 0029839845 scopus 로고    scopus 로고
    • A Bacillus subtilis gene cluster similar to the Escherichia coli phosphate-specific transport (pst) operon
    • Takemaru KI, Mizuno M & Kobayashi Y (1996) A Bacillus subtilis gene cluster similar to the Escherichia coli phosphate-specific transport (pst) operon. Microbiol. 142: 2017-2020
    • (1996) Microbiol. , vol.142 , pp. 2017-2020
    • Takemaru, K.I.1    Mizuno, M.2    Kobayashi, Y.3
  • 164
    • 0027538293 scopus 로고
    • Isolation and characterization of two immunochemically distinct alkaline phosphatases from Pseudomonas aeruginosa
    • Tan ASP & Worobec EA (1993) Isolation and characterization of two immunochemically distinct alkaline phosphatases from Pseudomonas aeruginosa. FEMS Microbiol. Lett. 106: 281-286
    • (1993) FEMS Microbiol. Lett. , vol.106 , pp. 281-286
    • Tan, A.S.P.1    Worobec, E.A.2
  • 165
    • 0027467289 scopus 로고
    • Inhibition of Escherichia coli chemotaxis by ω-conotoxin, a calcium ion channel blocker
    • Tisa LS, Olivera BM & Adler J (1993) Inhibition of Escherichia coli chemotaxis by ω-conotoxin, a calcium ion channel blocker. J. Bacteriol. 175: 1235-1238.
    • (1993) J. Bacteriol. , vol.175 , pp. 1235-1238
    • Tisa, L.S.1    Olivera, B.M.2    Adler, J.3
  • 166
    • 0342269112 scopus 로고
    • The birth and growth of the Pho regulon
    • Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) American Society for Microbiology, Washington, DC
    • Torriani-Gorini A (1987) The birth and growth of the Pho regulon. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A & Yagil E (Eds) Phosphate Metabolism and Cellular Regulation in Microorganisms, (pp 3-11). American Society for Microbiology, Washington, DC
    • (1987) Phosphate Metabolism and Cellular Regulation in Microorganisms , pp. 3-11
    • Torriani-Gorini, A.1
  • 170
    • 0027304422 scopus 로고
    • Mechanism and energetics of the secondary phosphate transport system of Acinetobacter johnsonii 210A
    • van Veen HW, Abee T, Kortstee GJJ, Konings WN & Zehnder AJB (1993b) Mechanism and energetics of the secondary phosphate transport system of Acinetobacter johnsonii 210A. J. Biol. Chem. 268: 19377-19383
    • (1993) J. Biol. Chem. , vol.268 , pp. 19377-19383
    • Van Veen, H.W.1    Abee, T.2    Kortstee, G.J.J.3    Konings, W.N.4    Zehnder, A.J.B.5
  • 171
    • 0028361375 scopus 로고
    • Substrate specificity of the two phosphate transport systems of Acinetobacter johnsonii 210A in relation to phosphate speciation in its aquatic environment
    • van Veen HW, Abee T, Kortstee GJJ, Konings WN & Zehnder AJB (1994a) Substrate specificity of the two phosphate transport systems of Acinetobacter johnsonii 210A in relation to phosphate speciation in its aquatic environment. J. Biol. Chem. 269: 16212-16216
    • (1994) J. Biol. Chem. , vol.269 , pp. 16212-16216
    • Van Veen, H.W.1    Abee, T.2    Kortstee, G.J.J.3    Konings, W.N.4    Zehnder, A.J.B.5
  • 172
    • 0028298054 scopus 로고
    • Translocation of metal phosphate via the phosphate inorganic transport (Pit) system of Escherichia coli
    • van Veen HW, Abee T, Kortstee GJJ, Konings WN & Zehnder AJB (1994b) Translocation of metal phosphate via the phosphate inorganic transport (Pit) system of Escherichia coli. Biochemistry 33: 1766-1770
    • (1994) Biochemistry , vol.33 , pp. 1766-1770
    • Van Veen, H.W.1    Abee, T.2    Kortstee, G.J.J.3    Konings, W.N.4    Zehnder, A.J.B.5
  • 173
    • 0013004377 scopus 로고
    • Phosphate inorganic transport (Pit) system inEscherichia coli and Acinetobacter johnsonii
    • Torriani-Gorini A, Yagil Y & Silver S (Eds) American Society for Microbiology, Washington, DC
    • van Veen HW, Abee T, Kortstee GJJ, Konings WN, & Zehnder AJB (1994c) Phosphate inorganic transport (Pit) system inEscherichia coli and Acinetobacter johnsonii. In: Torriani-Gorini A, Yagil Y & Silver S (Eds) Phosphate in Microorganisms: Cellular and Molecular Biology, (pp 43-49). American Society for Microbiology, Washington, DC
    • (1994) Phosphate in Microorganisms: Cellular and Molecular Biology , pp. 43-49
    • Van Veen, H.W.1    Abee, T.2    Kortstee, G.J.J.3    Konings, W.N.4    Zehnder, A.J.B.5
  • 174
    • 0028097447 scopus 로고
    • Generation of a proton motive force by the excretion of metal phosphate in the polyphosphate-accumulating Acinetobacter johnsonii strain 210A
    • van Veen HW, Abee T, Kortstee GJJ, Pereira H, Konings WN & Zehnder AJB (1994d) Generation of a proton motive force by the excretion of metal phosphate in the polyphosphate-accumulating Acinetobacter johnsonii strain 210A. J. Biol. Chem. 269: 29509-29514
    • (1994) J. Biol. Chem. , vol.269 , pp. 29509-29514
    • Van Veen, H.W.1    Abee, T.2    Kortstee, G.J.J.3    Pereira, H.4    Konings, W.N.5    Zehnder, A.J.B.6
  • 175
    • 0028297960 scopus 로고
    • Energetics of alanine, lysine and proline transport in cytoplasmic membranes of the polyphosphate-accumulating Acinetobacter johnsonii 210A
    • van Veen HW, Abee T, Kleefsman AWF, Melgers B, Kortstee GJJ, Konings WN & Zehnder AJB (1994e) Energetics of alanine, lysine and proline transport in cytoplasmic membranes of the polyphosphate-accumulating Acinetobacter johnsonii 210A. J. Bacteriol. 176: 2670-2776
    • (1994) J. Bacteriol. , vol.176 , pp. 2670-2776
    • Van Veen, H.W.1    Abee, T.2    Kleefsman, A.W.F.3    Melgers, B.4    Kortstee, G.J.J.5    Konings, W.N.6    Zehnder, A.J.B.7
  • 177
    • 0010720039 scopus 로고    scopus 로고
    • Functional complementation of the human multidrug resistance MDR1 gene by the bacterial antibiotic resistance ImrA gene
    • in press
    • van Veen HW, Callaghan R, Soceneantu L, Sardini A, Konings WN, Higgins CF (1997) Functional complementation of the human multidrug resistance MDR1 gene by the bacterial antibiotic resistance ImrA gene. Nature in press
    • (1997) Nature
    • Van Veen, H.W.1    Callaghan, R.2    Soceneantu, L.3    Sardini, A.4    Konings, W.N.5    Higgins, C.F.6
  • 178
    • 0021747364 scopus 로고
    • Cloning and expression in Escherichia coli K-12 of the structural gene for outer membrane PhoE protein from Enterobacter cloacae
    • Verhoef C, van Koppen C, Overduin P, Lugtenberg B, Korteland J & Tommassen J (1984) Cloning and expression in Escherichia coli K-12 of the structural gene for outer membrane PhoE protein from Enterobacter cloacae. Gene 32: 107-115
    • (1984) Gene , vol.32 , pp. 107-115
    • Verhoef, C.1    Van Koppen, C.2    Overduin, P.3    Lugtenberg, B.4    Korteland, J.5    Tommassen, J.6
  • 179
    • 0028027510 scopus 로고
    • Fine tuning the specificity of the periplasmic phosphate receptor
    • Wang Z, Choudhary A, Ledvina PS & Quiocho FA (1994) Fine tuning the specificity of the periplasmic phosphate receptor. J. Biol. Chem. 269: 25091-25094
    • (1994) J. Biol. Chem. , vol.269 , pp. 25091-25094
    • Wang, Z.1    Choudhary, A.2    Ledvina, P.S.3    Quiocho, F.A.4
  • 180
    • 0027411096 scopus 로고
    • Gene regulation by phosphate in enteric bacteria
    • Wanner BL (1993) Gene regulation by phosphate in enteric bacteria. J. Cell. Biochem. 51: 47-54
    • (1993) J. Cell. Biochem. , vol.51 , pp. 47-54
    • Wanner, B.L.1
  • 181
    • 0026560385 scopus 로고
    • Involvement of phosphotransacetylase, acetate kinase, and acetyl phosphate synthesis in control of the phosphate regulon in Escherichia coli
    • Wanner BL & Wilmes-Riesenberg MR (1992) Involvement of phosphotransacetylase, acetate kinase, and acetyl phosphate synthesis in control of the phosphate regulon in Escherichia coli. J. Bacteriol. 174: 2124-2130
    • (1992) J. Bacteriol. , vol.174 , pp. 2124-2130
    • Wanner, B.L.1    Wilmes-Riesenberg, M.R.2
  • 182
    • 0026491079 scopus 로고
    • Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters
    • Webb DC, Rosenberg H & Cox GB (1992) Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. J. Biol. Chem. 267: 24661-24668
    • (1992) J. Biol. Chem. , vol.267 , pp. 24661-24668
    • Webb, D.C.1    Rosenberg, H.2    Cox, G.B.3
  • 183
    • 0017597241 scopus 로고
    • Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium
    • Weppelman R, Kier LD & Ames BN (1977) Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium. J. Bacteriol. 130: 411-419
    • (1977) J. Bacteriol. , vol.130 , pp. 411-419
    • Weppelman, R.1    Kier, L.D.2    Ames, B.N.3
  • 184
    • 0023392218 scopus 로고
    • Identification of Uhp polypeptides and evidence for their role in exogenous induction of the sugar phosphate transport system of Escherichia coli
    • Weston LA & Kadner RJ (1987) Identification of Uhp polypeptides and evidence for their role in exogenous induction of the sugar phosphate transport system of Escherichia coli. J. Bacteriol. 169: 3546-3555
    • (1987) J. Bacteriol. , vol.169 , pp. 3546-3555
    • Weston, L.A.1    Kadner, R.J.2
  • 185
    • 0023812828 scopus 로고
    • Role of uhp genes in expression of the Escherichia coli sugar-phosphate transport system
    • Weston LA & Kadner RJ (1988) Role of uhp genes in expression of the Escherichia coli sugar-phosphate transport system. J. Bacteriol. 170: 3375-3383
    • (1988) J. Bacteriol. , vol.170 , pp. 3375-3383
    • Weston, L.A.1    Kadner, R.J.2
  • 186
    • 9844255244 scopus 로고
    • Coupled transport of citrate and magnesium in Bacillus subtilis
    • Willecke K, Grier E-M & Oehr P (1973) Coupled transport of citrate and magnesium in Bacillus subtilis. J. Bacteriol. 144: 366-374
    • (1973) J. Bacteriol. , vol.144 , pp. 366-374
    • Willecke, K.1    Grier, E.-M.2    Oehr, P.3
  • 187
    • 0016274285 scopus 로고
    • The loss of the phoS periplasmic protein leads to a change in the specificity of a constitutive inorganic phosphate transport system in Escherichia coli
    • Willsky GR & Malamy MH (1974) The loss of the phoS periplasmic protein leads to a change in the specificity of a constitutive inorganic phosphate transport system in Escherichia coli. Biochem. Biophys. Res. Commun. 60: 226-233
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 226-233
    • Willsky, G.R.1    Malamy, M.H.2
  • 188
    • 0019198011 scopus 로고
    • Characterization of two genetically separable inorganic phosphate transport systems in Escherichia coli
    • Willsky GR & Malamy MH (1980a) Characterization of two genetically separable inorganic phosphate transport systems in Escherichia coli. J. Bacteriol. 144: 356-365
    • (1980) J. Bacteriol. , vol.144 , pp. 356-365
    • Willsky, G.R.1    Malamy, M.H.2
  • 189
    • 0019163171 scopus 로고
    • Effect of arsenate on inorganic phosphate transport in Escherichia coli
    • Willsky GR & Malamy MH (1980b) Effect of arsenate on inorganic phosphate transport in Escherichia coli. J. Bacteriol. 144: 366-374
    • (1980) J. Bacteriol. , vol.144 , pp. 366-374
    • Willsky, G.R.1    Malamy, M.H.2
  • 190
    • 0015577495 scopus 로고
    • Inorganic phosphate transport in Escherichia coli: Involvement of two genes which play a role in alkaline phosphatase regulation
    • Willsky GR, Bennett RL & Malamy MH (1973) Inorganic phosphate transport in Escherichia coli: involvement of two genes which play a role in alkaline phosphatase regulation. J. Bacteriol. 113: 529-539
    • (1973) J. Bacteriol. , vol.113 , pp. 529-539
    • Willsky, G.R.1    Bennett, R.L.2    Malamy, M.H.3
  • 191
    • 0014030343 scopus 로고
    • A hexose-phosphate transport system in Escherichia coli
    • Winkler HH (1966) A hexose-phosphate transport system in Escherichia coli. Biochim. Biophys. Acta 117: 231-240
    • (1966) Biochim. Biophys. Acta , vol.117 , pp. 231-240
    • Winkler, H.H.1
  • 192
    • 0022868156 scopus 로고
    • Molecular aspects of inorganic phosphate transport in mitochondria
    • Wohlrab H (1986) Molecular aspects of inorganic phosphate transport in mitochondria. Biochim. Biophys. Acta 853: 115-134
    • (1986) Biochim. Biophys. Acta , vol.853 , pp. 115-134
    • Wohlrab, H.1
  • 193
    • 0025057276 scopus 로고
    • Regulation of the phosphate regulon of Escherichia coli: Properties of phoR deletion mutants and subcellular localization of PhoR protein
    • Yamada M, Makino K, Shinagawa H & Nakata A (1990) Regulation of the phosphate regulon of Escherichia coli: properties of phoR deletion mutants and subcellular localization of PhoR protein. Mol. Gen. Genet. 220: 366-372
    • (1990) Mol. Gen. Genet. , vol.220 , pp. 366-372
    • Yamada, M.1    Makino, K.2    Shinagawa, H.3    Nakata, A.4
  • 194
    • 0027484363 scopus 로고
    • Identification of a residue in the translocation pathway of a membrane carrier
    • Yan R-T & Maloney PC (1993) Identification of a residue in the translocation pathway of a membrane carrier. Cell 75: 37-44
    • (1993) Cell , vol.75 , pp. 37-44
    • Yan, R.-T.1    Maloney, P.C.2
  • 195
    • 0025148234 scopus 로고
    • Phosphatases of Acinetobacter Iwoffi. Localization and regulation of synthesis by orthophosphate
    • Yashphe J, Chikarmane H, Iranzo M & Halvorson HO (1990) Phosphatases of Acinetobacter Iwoffi. Localization and regulation of synthesis by orthophosphate. Curr. Microbiol. 20: 273-280
    • (1990) Curr. Microbiol. , vol.20 , pp. 273-280
    • Yashphe, J.1    Chikarmane, H.2    Iranzo, M.3    Halvorson, H.O.4
  • 197
    • 0029128358 scopus 로고
    • Non-physiological expression of UhpT does not lead to uncontrolled leakage of sugare phosphates out of Escherichia coli cells
    • van der Zee JR, Postma PW & Hellingwerf KJ (1995) Non-physiological expression of UhpT does not lead to uncontrolled leakage of sugare phosphates out of Escherichia coli cells. FEMS Microbiol. Lett. 131: 21-26
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 21-26
    • Van Der Zee, J.R.1    Postma, P.W.2    Hellingwerf, K.J.3
  • 198
    • 0023508150 scopus 로고
    • Phosphate transport in Halobacterium halobium depends on cellular ATP levels
    • Zoratti M & Lanyi JK (1987) Phosphate transport in Halobacterium halobium depends on cellular ATP levels. J. Bacteriol. 169: 5755-5760
    • (1987) J. Bacteriol. , vol.169 , pp. 5755-5760
    • Zoratti, M.1    Lanyi, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.