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Volumn 29, Issue 2, 1998, Pages 641-652

Limits to inducer exclusion: Inhibition of the bacterial phosphotransferase system by glycerol kinase

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA METHYLGLUCOSIDE; GLYCEROL; GLYCEROL KINASE; LACTIC ACID; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASE;

EID: 0031854376     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00963.x     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 0026509084 scopus 로고
    • Cyclic AMP in prokaryotes
    • Botsford, J.L., and Harman, J.G. (1992) Cyclic AMP in prokaryotes. Microbiol Rev 56: 100-122.
    • (1992) Microbiol Rev , vol.56 , pp. 100-122
    • Botsford, J.L.1    Harman, J.G.2
  • 2
    • 0015419787 scopus 로고
    • Deletion mapping of the genes coding for HPr and enzyme I of the phosphoenolpyruvate: Sugar phosphotransferase system in Salmonella typhimurium
    • Cordaro, J.C., and Roseman, S. (1972) Deletion mapping of the genes coding for HPr and enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system in Salmonella typhimurium. J Bacteriol 112: 17-29.
    • (1972) J Bacteriol , vol.112 , pp. 17-29
    • Cordaro, J.C.1    Roseman, S.2
  • 3
    • 0025687504 scopus 로고
    • Regulation of the maltose transport system of Escherichia coli by the glucose-specific Enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclusion in proteoliposomes
    • Dean, D.A., Reizer, J., Nikaido, H., and Saier, Jr, M.H. (1990) Regulation of the maltose transport system of Escherichia coli by the glucose-specific Enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclusion in proteoliposomes. J Biol Chem 265: 21005-21010.
    • (1990) J Biol Chem , vol.265 , pp. 21005-21010
    • Dean, D.A.1    Reizer, J.2    Nikaido, H.3    Saier Jr., M.H.4
  • 4
    • 0022531321 scopus 로고
    • Glc of the phosphoenolpyruvate: Carbohydrate phosphotransferase system
    • Glc of the phosphoenolpyruvate: carbohydrate phosphotransferase system. J Bacteriol 167: 393-395.
    • (1986) J Bacteriol , vol.167 , pp. 393-395
    • De Boer, M.1    Broekhuizen, C.P.2    Postma, P.W.3
  • 5
    • 0028334938 scopus 로고
    • Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation
    • Feese, M., Pettigrew, D.W., Meadow, N.D., Roseman, S., and Remington, S.J. (1994) Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Proc Natl Acad Sci USA 91: 3544-3548.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3544-3548
    • Feese, M.1    Pettigrew, D.W.2    Meadow, N.D.3    Roseman, S.4    Remington, S.J.5
  • 6
    • 0026802334 scopus 로고
    • Metabolic control analysis: A survey of its theoretical and experimental development
    • Fell, D.A. (1992) Metabolic control analysis: a survey of its theoretical and experimental development. Biochem J 286: 313-330.
    • (1992) Biochem J , vol.286 , pp. 313-330
    • Fell, D.A.1
  • 7
    • 0028360796 scopus 로고
    • Macromolecular crowding and confinement in cells exposed to hypertonicity
    • Garner, M.M., and Burg, M.B. (1994) Macromolecular crowding and confinement in cells exposed to hypertonicity. Am J Physiol 266: C877-C892.
    • (1994) Am J Physiol , vol.266
    • Garner, M.M.1    Burg, M.B.2
  • 8
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 9
    • 0039874703 scopus 로고
    • Studies on the glucose-transport system in Escherichia coli with α-methylglucoside as substrate
    • Hagihira, H., Wilson, T.H., and Lin, E.C.C. (1963) Studies on the glucose-transport system in Escherichia coli with α-methylglucoside as substrate. Biochim Biophys Acta 78: 505-515.
    • (1963) Biochim Biophys Acta , vol.78 , pp. 505-515
    • Hagihira, H.1    Wilson, T.H.2    Lin, E.C.C.3
  • 11
    • 0016609612 scopus 로고
    • The control by respiration of the uptake of α-methyl glucoside in Escherichia coli K12
    • Hernandez-Asensio, M., Ramirez, J.M., and del Campo, F.F. (1975) The control by respiration of the uptake of α-methyl glucoside in Escherichia coli K12. Arch Microbiol 103: 155-162.
    • (1975) Arch Microbiol , vol.103 , pp. 155-162
    • Hernandez-Asensio, M.1    Ramirez, J.M.2    Del Campo, F.F.3
  • 12
    • 9044252915 scopus 로고
    • Effect of metabolic activity on the glucose permease of bacterial cells
    • Hoffee, P., and Englesberg, E. (1962) Effect of metabolic activity on the glucose permease of bacterial cells. Proc Natl Acad Sci USA 48: 1759-1765.
    • (1962) Proc Natl Acad Sci USA , vol.48 , pp. 1759-1765
    • Hoffee, P.1    Englesberg, E.2
  • 14
    • 0015221227 scopus 로고
    • Local and non-local interactions of fluxes mediated by the glucose and galactose permeases of Escherichia coli
    • Koch, A.L. (1971) Local and non-local interactions of fluxes mediated by the glucose and galactose permeases of Escherichia coli. Biochim Biophys Acta 249: 197-215.
    • (1971) Biochim Biophys Acta , vol.249 , pp. 197-215
    • Koch, A.L.1
  • 15
    • 0025338715 scopus 로고
    • The bacterial phosphoenolpyruvate:glycose phosphotransferase system
    • Meadow, N.D., Fox, D.K., and Roseman, S. (1990) The bacterial phosphoenolpyruvate:glycose phosphotransferase system. Annu Rev Biochem 59: 497-542.
    • (1990) Annu Rev Biochem , vol.59 , pp. 497-542
    • Meadow, N.D.1    Fox, D.K.2    Roseman, S.3
  • 16
    • 0023665309 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. XXXII. Reconstitution of inducer exclusion in Salmonella typhimurium membrane vesicles
    • Misko, T.P., Mitchell, W.J., Meadow, N.D., and Roseman, S. (1987) Sugar transport by the bacterial phosphotransferase system. XXXII. Reconstitution of inducer exclusion in Salmonella typhimurium membrane vesicles. J Biol Chem 262: 16261-16266.
    • (1987) J Biol Chem , vol.262 , pp. 16261-16266
    • Misko, T.P.1    Mitchell, W.J.2    Meadow, N.D.3    Roseman, S.4
  • 18
    • 0000618190 scopus 로고
    • The mechanism of inducer exclusion. Direct interaction between purified IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system and the lactose carrier of Escherichia coli
    • Nelson, S.O., Wright, J.K., and Postma, P.W. (1983) The mechanism of inducer exclusion. Direct interaction between purified IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system and the lactose carrier of Escherichia coli. EMBO J 2: 715-720.
    • (1983) EMBO J , vol.2 , pp. 715-720
    • Nelson, S.O.1    Wright, J.K.2    Postma, P.W.3
  • 21
    • 0019983630 scopus 로고
    • Regulation of lactose permease activity by the phosphoenolpyruvate:sugar phosphotransferase system: Evidence for direct binding of the glucose-specific enzyme III to the lactose permease
    • Osumi, T., and Saier, Jr, M.H. (1982) Regulation of lactose permease activity by the phosphoenolpyruvate:sugar phosphotransferase system: Evidence for direct binding of the glucose-specific enzyme III to the lactose permease. Proc Natl Acad Sci USA 79: 1457-1461.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1457-1461
    • Osumi, T.1    Saier Jr., M.H.2
  • 22
    • 0024327471 scopus 로고
    • Regulation of Escherichia coli adenylate cyclase activity by the phosphoenolpyruvate:sugar phosphotransferase system
    • Peterkofsky, A., Svenson, I., and Amin, N. (1989) Regulation of Escherichia coli adenylate cyclase activity by the phosphoenolpyruvate:sugar phosphotransferase system. FEMS Microbiol Rev 63: 103-108.
    • (1989) FEMS Microbiol Rev , vol.63 , pp. 103-108
    • Peterkofsky, A.1    Svenson, I.2    Amin, N.3
  • 23
    • 0023879283 scopus 로고
    • Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme
    • Pettigrew, D.W., Ma, D.P., Conrad, C.A., and Johnson, J.R. (1988) Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme. J Biol Chem 263: 135-139.
    • (1988) J Biol Chem , vol.263 , pp. 135-139
    • Pettigrew, D.W.1    Ma, D.P.2    Conrad, C.A.3    Johnson, J.R.4
  • 24
    • 0017328510 scopus 로고
    • Galactose transport in Salmonella typhimurium
    • Postma, P.W. (1977) Galactose transport in Salmonella typhimurium. J Bacteriol 129: 630-639.
    • (1977) J Bacteriol , vol.129 , pp. 630-639
    • Postma, P.W.1
  • 25
    • 0018901629 scopus 로고
    • Enzymes II of the phosphotransferase system do not catalyze sugar transport in the absence of phosphorylation
    • Postma, P.W., and Stock, J.B. (1980) Enzymes II of the phosphotransferase system do not catalyze sugar transport in the absence of phosphorylation. J Bacteriol 141: 476-484.
    • (1980) J Bacteriol , vol.141 , pp. 476-484
    • Postma, P.W.1    Stock, J.B.2
  • 26
    • 0021288128 scopus 로고
    • Glc of the phosphoenolpyruvate:sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium
    • Glc of the phosphoenolpyruvate:sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium. J Bacteriol 158: 351-353.
    • (1984) J Bacteriol , vol.158 , pp. 351-353
    • Postma, P.W.1    Epstein, W.2    Schuitema, A.R.J.3    Nelson, S.O.4
  • 27
    • 15144353036 scopus 로고
    • Carbohydrate transport and metabolism in Escherichia coli and Salmonella typhimurium: Regulation by the PEP:carbohydrate phosphotransferase system
    • Palmieri, F., and Quagliariello, E. (eds). Amsterdam: Elsevier Science
    • Postma, P.W., Broekhuizen, C.P., Schuitema, A.R.J., Vogler, A.P., and Lengeler, J.W. (1988) Carbohydrate transport and metabolism in Escherichia coli and Salmonella typhimurium: regulation by the PEP:carbohydrate phosphotransferase system. In Molecular Basis of Biomembrane Transport. Palmieri, F., and Quagliariello, E. (eds). Amsterdam: Elsevier Science, pp. 43-52.
    • (1988) Molecular Basis of Biomembrane Transport , pp. 43-52
    • Postma, P.W.1    Broekhuizen, C.P.2    Schuitema, A.R.J.3    Vogler, A.P.4    Lengeler, J.W.5
  • 28
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma, P.W., Lengeler, J.W., and Jacobson, G.R. (1993) Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 57: 543-594.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 29
    • 0008550672 scopus 로고
    • Control of phosphoenolpyruvate-dependent phosphotransferase-mediated sugar transport in Escherichia coli by energization of the cell membrane
    • Reider, E., Wagner, E.F., and Schweiger, M. (1979) Control of phosphoenolpyruvate-dependent phosphotransferase-mediated sugar transport in Escherichia coli by energization of the cell membrane. Proc Natl Acad Sci USA 76: 5529-5533.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 5529-5533
    • Reider, E.1    Wagner, E.F.2    Schweiger, M.3
  • 30
    • 0030021703 scopus 로고    scopus 로고
    • Changes in the cellular energy state affect the activity of the bacterial phosphotransferase system
    • Rohwer, J.M., Jensen, P.R., Shinohara, Y., Postma, P.W., and Westerhoff, H.V. (1996) Changes in the cellular energy state affect the activity of the bacterial phosphotransferase system. Eur J Biochem 235: 225-230.
    • (1996) Eur J Biochem , vol.235 , pp. 225-230
    • Rohwer, J.M.1    Jensen, P.R.2    Shinohara, Y.3    Postma, P.W.4    Westerhoff, H.V.5
  • 31
    • 0020344951 scopus 로고
    • PEP: Glycose phosphotransferase system. General description and assay principles
    • Roseman, S., Meadow, N.D., and Kukuruzinska, M.A. (1982) PEP: glycose phosphotransferase system. General description and assay principles. Methods Enzymol 90: 417-423.
    • (1982) Methods Enzymol , vol.90 , pp. 417-423
    • Roseman, S.1    Meadow, N.D.2    Kukuruzinska, M.A.3
  • 32
    • 0024554141 scopus 로고
    • Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate: Sugar phosphotransferase system
    • Saier, Jr, M.H. (1989) Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Microbiol Rev 53: 109-120.
    • (1989) Microbiol Rev , vol.53 , pp. 109-120
    • Saier Jr., M.H.1
  • 33
    • 0026546539 scopus 로고
    • Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system
    • Saier, Jr, M.H., and Reizer, J. (1992) Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J Bacteriol 174: 1433-1438.
    • (1992) J Bacteriol , vol.174 , pp. 1433-1438
    • Saier Jr., M.H.A.1    Reizer, J.2
  • 34
    • 0017103194 scopus 로고
    • Sugar transport. X. Inducer exclusion and regulation of the melibiose, maltose, glycerol, and lactose transport systems by the phosphoenolpyruvate: Sugar phosphotransferase system
    • Saier, Jr, M.H., and Roseman, S. (1976) Sugar transport. X. Inducer exclusion and regulation of the melibiose, maltose, glycerol, and lactose transport systems by the phosphoenolpyruvate: sugar phosphotransferase system. J Biol Chem 251: 6606-6615.
    • (1976) J Biol Chem , vol.251 , pp. 6606-6615
    • Saier Jr., M.H.A.1    Roseman, S.2
  • 35
    • 0021030406 scopus 로고
    • Cooperative binding of the sugar substrates and allosteric regulatory protein (enzyme IIIGlc of the phosphotransferase system) to the lactose and melibiose permeases in Escherichia coli and Salmonella typhimurium
    • Saier, Jr, M.H., Novotny, M.J., Comeau-Fuhrman, D., Osumi, T., and Desai, J.D. (1983) Cooperative binding of the sugar substrates and allosteric regulatory protein (enzyme IIIGlc of the phosphotransferase system) to the lactose and melibiose permeases in Escherichia coli and Salmonella typhimurium. J Bacteriol 155: 1351-1357.
    • (1983) J Bacteriol , vol.155 , pp. 1351-1357
    • Saier Jr., M.H.1    Novotny, M.J.2    Comeau-Fuhrman, D.3    Osumi, T.4    Desai, J.D.5
  • 37
    • 0019497160 scopus 로고
    • Competition between two pathways for sugar uptake by the phosphoenolpyruvate-dependent sugar phosphotransferase system in Salmonella typhimurium
    • Scholte, B.J., and Postma, P.W. (1981) Competition between two pathways for sugar uptake by the phosphoenolpyruvate-dependent sugar phosphotransferase system in Salmonella typhimurium. Eur J Biochem 114: 51-58.
    • (1981) Eur J Biochem , vol.114 , pp. 51-58
    • Scholte, B.J.1    Postma, P.W.2
  • 38
    • 0019729083 scopus 로고
    • Isolation of IIIGIc of the phosphoenolpyruvate-dependent glucose phosphotransferase system of Salmonella typhimurium
    • Scholte, B.J., Schuitema, A.R., and Postma, P.W. (1981) Isolation of IIIGIc of the phosphoenolpyruvate-dependent glucose phosphotransferase system of Salmonella typhimurium. J Bacteriol 148: 257-264.
    • (1981) J Bacteriol , vol.148 , pp. 257-264
    • Scholte, B.J.1    Schuitema, A.R.2    Postma, P.W.3
  • 40
    • 0025058596 scopus 로고
    • Glycerol facilitator of Escherichia coli: Cloning of glpF and identification of the glpF product
    • Sweet, G., Gandor, C., Voegele, R., Wittekindt, N., Beuerle, J., Truniger, V., et al. (1990) Glycerol facilitator of Escherichia coli: cloning of glpF and identification of the glpF product. J Bacteriol 172: 424-430.
    • (1990) J Bacteriol , vol.172 , pp. 424-430
    • Sweet, G.1    Gandor, C.2    Voegele, R.3    Wittekindt, N.4    Beuerle, J.5    Truniger, V.6
  • 41
    • 0016410104 scopus 로고
    • Glycerol kinase
    • Thorner, J.W. (1975) Glycerol kinase. Methods Enzymol 42: 148-156.
    • (1975) Methods Enzymol , vol.42 , pp. 148-156
    • Thorner, J.W.1
  • 42
    • 0029049297 scopus 로고
    • Glc-like domain of IINag of the phosphotransferase system in Salmonella typhimurium LT2
    • Glc-like domain of IINag of the phosphotransferase system in Salmonella typhimurium LT2. Mol Gen Genet 248: 236-241.
    • (1995) Mol Gen Genet , vol.248 , pp. 236-241
    • Van Der Vlag, J.1    Postma, P.W.2
  • 43
    • 0028365828 scopus 로고
    • Glc of the phosphoenolpyruvate-dependent glucose phosphotransferase system in Salmonella typhimurium
    • Glc of the phosphoenolpyruvate-dependent glucose phosphotransferase system in Salmonella typhimurium. J Bacteriol 176: 3518-3526.
    • (1994) J Bacteriol , vol.176 , pp. 3518-3526
    • Van Der Vlag, J.1    Van Dam, K.2    Postma, P.W.3
  • 44
    • 0029016352 scopus 로고
    • Control of glucose metabolism by the enzymes of the glucose phosphotransferase system in Salmonella typhimurium
    • van der Vlag, J., van't Hof, R., van Dam, K., and Postma, P.W. (1995) Control of glucose metabolism by the enzymes of the glucose phosphotransferase system in Salmonella typhimurium. Eur J Biochem 230: 170-182.
    • (1995) Eur J Biochem , vol.230 , pp. 170-182
    • Van Der Vlag, J.1    Van't Hof, R.2    Van Dam, K.3    Postma, P.W.4
  • 46
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman, S.B., and Minton, A.P. (1993) Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu Pev Biophys Biomol Struct 22: 27-65.
    • (1993) Annu Pev Biophys Biomol Struct , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 47
    • 0014802916 scopus 로고
    • Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli
    • Zwaig, N., Kistler, W.S., and Lin, E.C.C. (1970) Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli. J Bacteriol 102: 753-759.
    • (1970) J Bacteriol , vol.102 , pp. 753-759
    • Zwaig, N.1    Kistler, W.S.2    Lin, E.C.C.3


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