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Volumn 183, Issue 11, 2001, Pages 3336-3344

Reverse genetics of escherichia coli glycerol kinase allosteric regulation and glucose control of glycerol utilization in vivo

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE 1,6 BISPHOSPHATE; GLUCOSE; GLYCEROL; GLYCEROL KINASE;

EID: 0035026474     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.183.11.3336-3344.2001     Document Type: Article
Times cited : (41)

References (42)
  • 1
  • 2
    • 0014980547 scopus 로고
    • Glycerol-specific revertants of a phosphoenolpyruvate phosphotransferase mutant: Suppression by the desensitization of glycerol kinase to feedback inhibition
    • Berman, M., and E. C. C. Lin. 1971. Glycerol-specific revertants of a phosphoenolpyruvate phosphotransferase mutant: suppression by the desensitization of glycerol kinase to feedback inhibition. J. Bacteriol. 105:113-120.
    • (1971) J. Bacteriol. , vol.105 , pp. 113-120
    • Berman, M.1    Lin, E.C.C.2
  • 3
    • 0033802606 scopus 로고    scopus 로고
    • Purification and characterization of glpX-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli
    • Donahue, J. L., J. L. Bownas, W. G. Niehaus, and T. J. Larson. 2000. Purification and characterization of glpX-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli. J. Bacteriol. 182:5624-5627.
    • (2000) J. Bacteriol. , vol.182 , pp. 5624-5627
    • Donahue, J.L.1    Bownas, J.L.2    Niehaus, W.G.3    Larson, T.J.4
  • 4
    • 0032533833 scopus 로고    scopus 로고
    • Glycerol kinase from Escherichia coli and an Ala65→Thr mutant - The crystal structures reveal conformational changes with implications for allosteric regulation
    • Feese, D. M., H. R. Faber, C. E. Bystrom, D. W. Pettigrew, and S. J. Remington. 1998. Glycerol kinase from Escherichia coli and an Ala65→Thr mutant - the crystal structures reveal conformational changes with implications for allosteric regulation. Structure 6:1407-1418.
    • (1998) Structure , vol.6 , pp. 1407-1418
    • Feese, D.M.1    Faber, H.R.2    Bystrom, C.E.3    Pettigrew, D.W.4    Remington, S.J.5
  • 5
    • 0000661051 scopus 로고    scopus 로고
    • Organization and function of transcription regulatory elements
    • F. C. Neidhardt (ed.), ASM Press, Washington, D.C.
    • Gralla, J. D., and J. Collado-Vides. 1996. Organization and function of transcription regulatory elements, p. 1232-1245. In F. C. Neidhardt (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 1, ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 1232-1245
    • Gralla, J.D.1    Collado-Vides, J.2
  • 9
    • 0035140101 scopus 로고    scopus 로고
    • Unexpected presence of defective glpR alleles in various strains of Escherichia coli
    • Holtman, C. K., R. Thurlkill, and D. W. Pettigrew. 2001. Unexpected presence of defective glpR alleles in various strains of Escherichia coli. J. Bacteriol. 183:1459-1461.
    • (2001) J. Bacteriol. , vol.183 , pp. 1459-1461
    • Holtman, C.K.1    Thurlkill, R.2    Pettigrew, D.W.3
  • 11
    • 0030089476 scopus 로고    scopus 로고
    • Mechanism responsible for glucoselactose diauxie in Escherichia coli: Challenge to the cAMP model
    • Inada,T., K. Kimata, and H. Aiba. 1996. Mechanism responsible for glucoselactose diauxie in Escherichia coli: challenge to the cAMP model. Genes Cells 1:293-301.
    • (1996) Genes Cells , vol.1 , pp. 293-301
    • Inada, T.1    Kimata, K.2    Aiba, H.3
  • 12
    • 0016265088 scopus 로고
    • Genetic control of inducer exclusion by escherichia coli
    • Jones-Mortimer, M. C., and H. L. Kornberg. 1974. Genetic control of inducer exclusion by Escherichia coli. FEBS Lett. 48:93-95.
    • (1974) FEBS Lett. , vol.48 , pp. 93-95
    • Jones-Mortimer, M.C.1    Kornberg, H.L.2
  • 13
    • 0026660358 scopus 로고
    • Interaction at a distance between multiple operators controls the adjacent, divergently transcribed glpTQ-glpACB operons of Escherichia coli K-12
    • Larson, T. J., J. S. Cantwell, and A. T. van Loo-Bhattacharya. 1992. Interaction at a distance between multiple operators controls the adjacent, divergently transcribed glpTQ-glpACB operons of Escherichia coli K-12. J. Biol. Chem. 267:6114-6121.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6114-6121
    • Larson, T.J.1    Cantwell, J.S.2    Van Loo-Bhattacharya, A.T.3
  • 14
    • 0000071066 scopus 로고    scopus 로고
    • Dissimilatory pathways for sugars, polyois, and carboxylates
    • In F. C. Neidhardt (ed.). ASM Press, Washington, D.C.
    • Lin, E. C. C. 1996. Dissimilatory pathways for sugars, polyois, and carboxylates, p. 307-342. In F. C. Neidhardt (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. I. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 307-342
    • Lin, E.C.C.1
  • 15
    • 0017243175 scopus 로고
    • Glycerol dissimilation and its regulation in bacteria
    • Lin, E. C. C. 1976. Glycerol dissimilation and its regulation in bacteria. Annu. Rev. Microbiol. 30:535-578.
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 535-578
    • Lin, E.C.C.1
  • 17
    • 0018562382 scopus 로고
    • A multipurpose cloning system based on the single-stranded DNA bacteriophage M13
    • NIH publication no. 79-99, National Institutes of Health, Bethesda, Md.
    • Messing, J. 1979. A multipurpose cloning system based on the single-stranded DNA bacteriophage M13. Recombinant DNA technical bulletin. NIH publication no. 79-99, vol. 2, p. 43-48. National Institutes of Health, Bethesda, Md.
    • (1979) Recombinant DNA Technical Bulletin , vol.2 , pp. 43-48
    • Messing, J.1
  • 18
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N. Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N. Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 20
    • 0032564319 scopus 로고    scopus 로고
    • Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate
    • Ormo, M., C. E. Bystrom, and S. J. Remington. 1998. Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate. Biochemistry 37:16565-16572.
    • (1998) Biochemistry , vol.37 , pp. 16565-16572
    • Ormo, M.1    Bystrom, C.E.2    Remington, S.J.3
  • 21
    • 0345643778 scopus 로고    scopus 로고
    • A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo
    • Pettigrew, D. W., W. Z. Liu, C. Holmes, N. D. Meadow, and S. Roseman. 1996. A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo. J. Bacteriol. 178:2846-2852.
    • (1996) J. Bacteriol. , vol.178 , pp. 2846-2852
    • Pettigrew, D.W.1    Liu, W.Z.2    Holmes, C.3    Meadow, N.D.4    Roseman, S.5
  • 22
    • 0023879283 scopus 로고
    • Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme
    • Pettigrew, D. W., D.-P. Ma, C. A. Conrad, and J. R. Johnson. 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
  • 23
    • 0032492662 scopus 로고    scopus 로고
    • Glc with regulatory target protein glycerol kinase - Substitutions of a zinc(II) ligand and implications for inducer exclusion
    • Glc with regulatory target protein glycerol kinase - substitutions of a zinc(II) ligand and implications for inducer exclusion. Biochemistry 37:4875-4883.
    • (1998) Biochemistry , vol.37 , pp. 4875-4883
    • Pettigrew, D.W.1    Meadow, N.D.2    Roseman, S.3    Remington, S.J.4
  • 24
    • 0032518195 scopus 로고    scopus 로고
    • Conserved active site aspartates and domain-domain interactions in regulatory properties of the sugar kinase superfamily
    • Pettigrew, D. W., G. B. Smith, K. P. Thomas, and D. C. Dodds. 1998. Conserved active site aspartates and domain-domain interactions in regulatory properties of the sugar kinase superfamily. Arch. Biochem. Biophys. 349:236-245.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 236-245
    • Pettigrew, D.W.1    Smith, G.B.2    Thomas, K.P.3    Dodds, D.C.4
  • 25
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low-molecular-weight solutes
    • Philo, J. S. 1997. An improved function for fitting sedimentation velocity data for low-molecular-weight solutes. Biophys. J. 72:435-444.
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.S.1
  • 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
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:Carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 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
  • 28
    • 0343424366 scopus 로고    scopus 로고
    • Retro-regulation of the bacterial phosphotransferase system: A kinetic model
    • C. Larsson, I.-L. Påhlman, and L. Gustafsson (ed.), Biothermokinetics in the post genomic era. Göteborg University, Göteborg, Sweden
    • Rohwer, J. M., J.-H. S. Hofmeyr, and P. W. Postma. 1998. Retro-regulation of the bacterial phosphotransferase system: a kinetic model, p. 340-344. In C. Larsson, I.-L. Påhlman, and L. Gustafsson (ed.), Biothermokinetics in the post genomic era. Proceedings of the 8th International Meeting on BioThermoKinetics, Göteborg University, Göteborg, Sweden.
    • (1998) Proceedings of the 8th International Meeting on BioThermokinetics , pp. 340-344
    • Rohwer, J.M.1    Hofmeyr, J.-H.S.2    Postma, P.W.3
  • 29
    • 0343860134 scopus 로고
    • The bacterial phosphoenolpyruvate:Glycose phosphotransferase system
    • A. Torriani-Gorini, E. Yagil, and S. Silver (ed.). ASM Press, Washington, D.C.
    • Roseman, S. 1994. The bacterial phosphoenolpyruvate:glycose phosphotransferase system, p. 151-160. In A. Torriani-Gorini, E. Yagil, and S. Silver (ed.). Phosphate in microorganisms: cellular and molecular biology. ASM Press, Washington, D.C.
    • (1994) Phosphate in Microorganisms: Cellular and Molecular Biology , pp. 151-160
    • Roseman, S.1
  • 30
    • 0025233875 scopus 로고
    • Signal transduction by the bacterial phosphotransferase system. Diauxie and the crr gene
    • Roseman, S., and N. D. Meadow. 1990. Signal transduction by the bacterial phosphotransferase system. Diauxie and the crr gene. J. Biol. Chem. 265: 2993-2996.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2993-2996
    • Roseman, S.1    Meadow, N.D.2
  • 31
    • 0023665338 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsl, and crr genes
    • Saffen, D. W., K. A. Presper, T. L. Doering, and S. Roseman. 1987. Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsl, and crr genes. J. Biol. Chem. 262:16241-16253.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16241-16253
    • Saffen, D.W.1    Presper, K.A.2    Doering, T.L.3    Roseman, S.4
  • 32
    • 0024554141 scopus 로고
    • Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate:Sugar phosphotransferase system
    • Saier, M. H., Jr. 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 M.H., Jr.1
  • 33
    • 0017802555 scopus 로고
    • Permease-specific mutations in Salmonella typhimurium and Escherichia coli that release the glycerol, maltose, melibiose, and lactose transport systems from regulation by the phosphoenolpyruvate:Sugar phosphotransferase system
    • Saier, M. H., Jr., H. Straud, L. S. Massman, J. J. Judice, M. J. Newman, and B. U. Feucht. 1978. Permease-specific mutations in Salmonella typhimurium and Escherichia coli that release the glycerol, maltose, melibiose, and lactose transport systems from regulation by the phosphoenolpyruvate:sugar phosphotransferase system. J. Bacteriol. 133:1358-1367.
    • (1978) J. Bacteriol. , vol.133 , pp. 1358-1367
    • Saier M.H., Jr.1    Straud, H.2    Massman, L.S.3    Judice, J.J.4    Newman, M.J.5    Feucht, B.U.6
  • 35
    • 0022719327 scopus 로고
    • pHG165: A pBr322 copy number derivative of pUC8 for cloning and expression
    • Stewart, G. A. B., S. Lubinsky-Mink, C. G. Jackson, A. Cassel, and J. Kuhn. 1986. pHG165: a pBR322 copy number derivative of pUC8 for cloning and expression. Plasmid 15:172-181.
    • (1986) Plasmid , vol.15 , pp. 172-181
    • Stewart, G.A.B.1    Lubinsky-Mink, S.2    Jackson, C.G.3    Cassel, A.4    Kuhn, J.5
  • 36
    • 0033118267 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria
    • Stulke, J., and W. Hillen. 1999. Carbon catabolite repression in bacteria. Curr. Opin. Microbiol. 2:195-201.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 195-201
    • Stulke, J.1    Hillen, W.2
  • 37
    • 0026702038 scopus 로고
    • Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12
    • Weissenborn, D. L., N. Wittekindt, and T. J. Larson. 1992. Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12. J. Biol. Chem. 267:6122-6131.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6122-6131
    • Weissenborn, D.L.1    Wittekindt, N.2    Larson, T.J.3
  • 38
    • 0030914635 scopus 로고    scopus 로고
    • Action at a distance for glp repressor control of glpTQ transcription in Escherichia coli K-12
    • Yang, B., S. G. Gerhardt, and T. J. Larson. 1997. Action at a distance for glp repressor control of glpTQ transcription in Escherichia coli K-12. Mol. Microbiol. 24:511-521.
    • (1997) Mol. Microbiol. , vol.24 , pp. 511-521
    • Yang, B.1    Gerhardt, S.G.2    Larson, T.J.3
  • 39
    • 0032481591 scopus 로고    scopus 로고
    • Multiple promoters are responsible for transcription of the glpEGR operon of Escherichia coli K-12
    • Yang, B., and T. J. Larson. 1998. Multiple promoters are responsible for transcription of the glpEGR operon of Escherichia coli K-12. Biochim. Biophys. Acta 1396:114-126.
    • (1998) Biochim. Biophys. Acta , vol.1396 , pp. 114-126
    • Yang, B.1    Larson, T.J.2
  • 40
    • 0028348309 scopus 로고
    • Characterization of the interaction of the glp repressor of Escherichia coli K-12 with single and tandem glp operator variants
    • Zhao, N., W. Oh, D. Trybul, K. S. Thrasher, T. J. Kingsbury, and T. J. Larson. 1994. Characterization of the interaction of the glp repressor of Escherichia coli K-12 with single and tandem glp operator variants. J. Bacteriol. 176:2393-2397.
    • (1994) J. Bacteriol. , vol.176 , pp. 2393-2397
    • Zhao, N.1    Oh, W.2    Trybul, D.3    Thrasher, K.S.4    Kingsbury, T.J.5    Larson, T.J.6
  • 41
    • 0014802916 scopus 로고
    • Glycerol kinase, the pacemaker for the dissimilation of glycerol in Escherichia coli
    • Zwaig, N., W. S. Kistler, and E. C. C. Lin. 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
  • 42
    • 0014013188 scopus 로고
    • Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia coli
    • Zwaig, N., and E. C. C. Lin. 1966. Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia coli. Science 153:755-757.
    • (1966) Science , vol.153 , pp. 755-757
    • Zwaig, N.1    Lin, E.C.C.2


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