The Phosphoenolpyruvate-Dependent Carbohydrate: Phosphotransferase System (PTS) and Control of Carbon Source Utilization

  • Joseph W. Lengeler


Unicellular microorganisms such as Escherichia coli must be able to detect changes in their environment and to adapt their metabolism rapidly to external fluctuations. Adaptation of bacterial populations to such changes is in general transient, i.e., the cellular adaptation persists not much longer than the environmental change lasts and will be accommodated during a prolonged change. Prokaryotes monitor their surroundings directly by membrane-bound sensors, and indirectly by intracellular sensors which detect changes in pools of intracellular metabolites that vary as the consequence of extracellular changes. The pools usually correlate with the transport capacity of a cell. Most sensors are linked through complex signal transduction pathways to global regulatory networks. Global control systems, however, regulate metabolic networks, e.g., those involved in carbon source utilization, cellular differentiation processes, and the behavior of bacterial populations. Their activity leads eventually to the adaptation of cells to the change in conditions. Formally speaking, bacterial adaptation and differentiation processes can be viewed in analogy to other transiently acting sensory processes, and the entire bacterial cell may thus be seen as the equivalent of a transiently responding sensory system.


Adenylate Cyclase Catabolite Repression Carbon Catabolite Repression Carbon Source Utilization Phosphotransferase System 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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  1. 1.
    Monod J. Recherches sur la croissance des cultures bactériennes. Hermann et Cie, Paris. 1942.Google Scholar
  2. 2.
    Magasanik B. Catabolite repression. Cold Spring Harbor Symp Quant Biol 1961; 26:249–256.Google Scholar
  3. 3.
    Magasanik B. Glucose effects: Inducer exclusion and repression. In: Beckwith JR, Zipser D eds. The lactose Operon. Cold Spring Harbor, NY: Cold Spring Harbor, 1970; 189–219.Google Scholar
  4. 4.
    Paigen K, Williams B. Catabolite repression and other control mechanisms in carbohydrate utilization. Adv Microb Physiol 1970; 4:251–324.Google Scholar
  5. 5.
    Pastan I, Adhya S. Cyclic adenosine 3′-5′-monophosphate in Escherichia coli. Bacteriol Rev 1976; 40:527–551.Google Scholar
  6. 6.
    Lin ECC. The genetics of bacterial transport systems. Annu Rev Genet 1970; 4:225–262.Google Scholar
  7. 7.
    Kundig W, Gosh S, Roseman S. Phosphate bound to histidine in a protein as an intermediate in a novel phospho-transferase system. Proc Natl Acad Sci USA 1964; 52:1067–1074.Google Scholar
  8. 8.
    Postma PW, Roseman S. The bacterial phosphoenolpyruvate:sugar phosphotransferase system. Biochim Biophys Acta 1976; 457:213–257.Google Scholar
  9. 9.
    Saier Jr MH, Roseman S. Sugar transport. Inducer exclusion and regulation of the melibiose, maltose, glycerol, and lactose transport systems by the phosphoenol-pyruvate:sugar phosphotransferase system. J Biol Chem 1976; 251:6606–6615.Google Scholar
  10. 10.
    Saier Jr MH, Roseman S. Sugar transport. The crr mutation: its effect on repression of enzyme synthesis. J Biol Chem 1976; 251:6598–6605.Google Scholar
  11. 11.
    Kolb A, Busby S, Buc H et al. Transcriptional regulation by cAMP and its receptor protein. Annu Rev Biochem 1993; 62:749–795.Google Scholar
  12. 12.
    Postma PW, Lengeler JW, Jacobson GR. Phosphoenolpyruvate:car-bohydrate phosphotransferase systems of bacteria. Microbiol Rev 1993 57:543–594.Google Scholar
  13. 13.
    Gottesman S. Bacterial regulation: global regulatory networks. Ann Rev Genet 1984; 18:415–441.Google Scholar
  14. 14.
    Lengeler JW, Bettenbrock K, Lux R. Signal transduction through phosphotransferase systems or PTSs. In: Torriani-Gorini AM, Yagil E, Silver S, eds. Phosphate in Microorganisms. Cellular and Molecular Biology. Washington: ASM Press, 1994:192–188.Google Scholar
  15. 15.
    Roseman S, Meadow, ND. Signal transduction by the bacterial phosphotransferase system. J Biol Chem 1990; 265:2993–2996.Google Scholar
  16. 16.
    Postma PW, Lengeler JW. Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria. Microbiol Rev 1985; 49:232–269.Google Scholar
  17. 17.
    Kornberg HL. Fine control of sugar uptake by Escherichia coli. Symp Soc Exp Biol 1973; 27:175–193.Google Scholar
  18. 18.
    Berman M, Lin ECC. Glycerol-specific revenants of a phosphoenolpyruvate phosphotransferase mutant: suppression by the desensitization of glycerol kinase to feedback inhibition. J Bacteriol 105: 113–120.Google Scholar
  19. 19.
    Lengeler J, Lin ECC. Reversal of the mannitol-sorbitol diauxie in Escherichia coli. J Bacteriol 1972; 112:840–848.Google Scholar
  20. 20.
    Botsford JL, Harman JG. Cyclic AMP in prokaryotes. Microbiol Rev 1992; 56:100–122.Google Scholar
  21. 21.
    Pastan I, Perlman RL. Repression of ß-galactosidase synthesis by glucose in phosphotransferase mutants of Escherichia coli. Repression in the absence of glucose phosphorylation. J Biol Chem 1969; 244:5836–5842.Google Scholar
  22. 22.
    Pastan I, Perlman RL. Cyclic adenosine monophosphate in bacteria. Science 1970; 169:339–344.Google Scholar
  23. 23.
    Epstein W, Rothman-Denes LB, Hesse J. Adenosine 3′:5′-cyclic monophosphate as mediator of catabolite repression in Escherichia coli. Proc Natl Acad Sci USA 1975; 72:2300–2304.Google Scholar
  24. 24.
    Iuchi S, Lin ECC. arcA (dye), a global regulatory gene in Escherichia coli, mediating repression of enzymes in aerobic pathways. Proc Natl Acad Sci USA 1988; 85:1888–1892.Google Scholar
  25. 25.
    Neidhardt FC, Ingraham JL, Schaechter M. Physiology of the bacterial cell. A molecular approach. Sunderland, Massachusetts: Sinauer Associates, Inc. 1990.Google Scholar
  26. 26.
    Parkinson JS. Signal transduction schemes of bacteria. Cell 1993; 73:857–871.Google Scholar
  27. 27.
    Stock J. Phosphoprotein talk. Curr Biol 1993; 3:303–305.Google Scholar
  28. 28.
    Meadow ND, Fox DK, Roseman S. The bacterial phosphoenol-pyruvate:glycose phosphotransferase system. Ann Rev Biochem 1990; 59:497–542.Google Scholar
  29. 29.
    Robillard GT, Lolkema JS. Enzymes II of the phosphoenolpyruvate-de-pendent sugar transport systems: a review of their structure and mechanism of sugar transport. Biochim Biophys Acta 1988; 947:493–519.Google Scholar
  30. 30.
    Tanaka S, Lin ECC. Two classes of pleiotropic mutants of Aerobacter aerogenes lacking components of a phosphoenolpyruvate-dependent phosphotransferase system. Proc Natl Acad Sci USA 1967; 57:913–919.Google Scholar
  31. 31.
    Lengeler JW, Jahreis K, Wehmeier UF. Enzymes II of the phosphoenolpyruvate-dependent phosphotransferase systems: their structure and function in carbohydrate transport. Biochim Biophys Acta 1994; 1188:1–28.Google Scholar
  32. 32.
    Sharma S, Georges F, Delbaere LTJ et al. Epitope mapping by mutagenesis distinguishes between the two tertiary structures of the histidine-con-taining protein HPr. Proc Natl Acad Sci USA 1991; 88:4877–4881.Google Scholar
  33. 33.
    Worthylake D, Meadow ND, Roseman S et al. Three-dimensional structure of the Escherichia coli phosphocarrier protein III. Proc Natl Acad Sci USA 1991; 88:10382–10386.Google Scholar
  34. 34.
    Presper KA, Wong CY, Liu L et al. Site-directed mutagenesis of the phosphocarrier protein, IIIGlc, a major signal-transducing protein in Escherichia coli. Proc Natl Acad Sci USA 1989; 86:4052–4055.Google Scholar
  35. 35.
    Van Nuland NAJ, Kroon GJA, Dijkstra K et al. The NMR determination of the IIAMtl binding site on HPr of the Escherichia coli phospho-enolpyruvate-dependent phospho-transferase system. FEBS Lett 1993; 315:11–15.Google Scholar
  36. 36.
    Saier Jr MH, Roseman S. Inducer exclusion and repression of enzyme synthesis in mutants of Salmonella typhimurium defective in enzyme I of the phosphoenol-pyruvate:sugar phosphotransferase system. J Biol Chem 1972; 247:972–975.Google Scholar
  37. 37.
    Castro L, Feucht BU, Morse ML et al. Regulation of carbohydrate permeases and adenylate cyclase in Escherichia coli. Studies with mutant strains in which Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system is thermolabile. J Biol Chem 1976; 251:5522–5527.Google Scholar
  38. 38.
    Kornberg HL, Watts PD. Roles of crr-gene products in regulating carbohydrate uptake by Escherichia coli. FEBS Lett 1978; 89:329–339.Google Scholar
  39. 39.
    Nelson SO, Lengeler J, Postma PW. Role of IIIGlc of the phosphoenolpyru-vate-glucose phosphotransferase system in inducer exclusion in Escherichia coli. J Bacteriol 1984; 160:360–364.Google Scholar
  40. 40.
    Peterkofsky A, Svenson I, Amin N. Regulation of Escherichia coli adenylate cyclase activity by the phosphoenolpyruvate: sugar phosphotransferase system. FEMS Microbiol Rev 1989; 63:103–108.Google Scholar
  41. 41.
    Feucht BU, Saier MH Jr. Fine control of adenylate cyclase by the phosphoenolpyruvate: sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium. J Bacteriol 1980; 141:603–610.Google Scholar
  42. 42.
    Nelson SO, Scholte BJ, Postma PW. Phosphoenolpyruvate:sugar phosphotransferase system-mediated regulation of carbohydrate metabolism in Salmonella typhimurium. J Bacteriol 1982; 150:604–615.Google Scholar
  43. 43.
    Harwood JP, Gazdar C, Prasad C et al. Involvement of the glucose enzymes II of the sugar phosphotransferase system in the regulation of adenylate cyclase by glucose in Escherichia coli. J Biol Chem 1976; 251:2462–2468.Google Scholar
  44. 44.
    . Parra F, Jones-Mortimer MC, Kornberg HL. Phosphotransferase-mediated regulation of carbohydrate utilization in Escherichia coli K12: the nature of the iex (crr) and gsr (tgs) mutations. J Gen Microbiol 1983; 129:337–348.Google Scholar
  45. 45.
    Reddy P, Meadow N, Roseman S et al. Reconstitution of regulatory properties of adenylate cyclase in Escherichia coli extracts. Proc Natl Acad Sci USA 1985; 82:8300–8304.Google Scholar
  46. 46.
    . Liberman E, Saffen D, Roseman S et al. Inhibition of E. coli adenylate cyclase activity by inorganic orthophosphate is dependent on IIIGlc of the phosphoenolpyruvate:glycose phosphotransferase system. Biochem Biophys Res Commun 1986; 141:1138–1144.Google Scholar
  47. 47.
    . Magasanik B, Neidhardt F. Regulation of carbon and nitrogen utilization. In: Neidhardt F, ed. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. Washington, DC: ASM, 1987:1318–1325.Google Scholar
  48. 48.
    Ullmann A, Danchin A. Role of cyclic AMP in bacteria. Adv Cyclic Nucleotide Res 1983; 15:2–53.Google Scholar
  49. 49.
    Wanner BL, Kodaira R, Neidhardt FC. Regulation of lac Operon expression: reappraisal of the theory of catabolite repression. J Bacteriol 1978; 136:947–954.Google Scholar
  50. 50.
    Botsford JL, Drexler M. The cyclic 3′,5′-adenosine monophosphate receptor protein and regulation of cyclic 3′,5′-adenosine monophosphate synthesis in Escherichia coli. Mol Gen Genet 1978; 165:47–56.Google Scholar
  51. 51.
    Potter K, Chaloner-Larsson G, Yamazaki H. Abnormally high rate of cyclic AMP excretion from an Escherichia coli mutant deficient in cyclic AMP receptor protein. Biochem Biophys Res Commun 1974; 57:379–385.Google Scholar
  52. 52.
    Crasnier M, Danchin A. Characterization of Escherichia coli adenylate cyclase mutants with modified regulation. J Gen Microbiol 1990; 136:1825–1831.Google Scholar
  53. 53.
    Den Blaauwen JL, Postma PW. Regulation of cyclic AMP synthesis by enzyme IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system in crp strains of Salmonella typhimurium. J Bacteriol 1985; 164:477–478.Google Scholar
  54. 54.
    Fandl JP, Thorner LK, Artz SW. Mutations that affect transcription and cyclic AMP-CRP regulation of the adenylate cyclase gene (cya) of Salmonella typhimurium. Genetics 1990; 125:719–727.Google Scholar
  55. 55.
    Joseph E, Bernsley C, Guiso N et al. Multiple regulation of the activity of adenylate cyclase in Escherichia coli. Mol Gen Genet 1982; 185:262–268.Google Scholar
  56. 56.
    Saier Jr MH, Feucht BU, McCaman MT. Regulation of intracellular adenosine cyclic 3′:5′-monophosphate levels in Escherichia coli and Salmonella typhimurium. Evidence for energy-dependent excretion of the cyclic nucleotide. J Biol Chem 1975; 250:7593–7601.Google Scholar
  57. 57.
    Crasnier M, Dumay V, Danchin A. The catalytic domain of Escherichia coli K-12 adenylate cyclase as revealed by deletion analysis of the cya gene. Mol Gen Genet 1994; 243:409–416.Google Scholar
  58. 58.
    Ishizuka H, Hanamura A, Inada T et al. Mechanism of the down-regulation of cAMP receptor protein by glucose in Escherichia coli: role of autoregulation of the crp gene. EMBO J 1994; 13:3077–3082.Google Scholar
  59. 59.
    Ishizuka H, Hanamura A, Kunimura T et al. A lowered concentration of cAMP receptor protein caused by glucose is an important determinant for catabolite repression in Escherichia coli. Molec Microbiol 1993; 10:341–350.Google Scholar
  60. 60.
    Crenon I, Ullmann A. The role of cyclic AMP excretion in the regulation of enzyme synthesis in Escherichia coli. FEMS Microbiol Lett 1984; 22:47–51.Google Scholar
  61. 61.
    Saier Jr MH. Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyru-vate:sugar phosphotransferase system. Microbiol Rev 1989; 53:109–120.Google Scholar
  62. 62.
    Mitchell WJ, Saffen DW, Roseman S. Sugar transport by the bacterial phosphotransferase system. In vivo regulation of lactose transport in Escherichia coli by IIIG1c, a protein of the phosphoenolpyruvate:glycose phosphotransferase system. J Biol Chem 1987; 262:16254–16260.Google Scholar
  63. 63.
    Nelson SO, Wright JK, Postma PW. The mechanism of inducer exclusion. Direct interaction between purified IIIG1c of the phospho-enolpyruvate:sugar phosphotransferase system and the lactose carrier of Escherichia coli. EMBO J 1983; 2:715–720.Google Scholar
  64. 64.
    Osumi T, Saier Jr MH. Regulation of lactose permease activity by the phosphoenol-pyruvate:sugar phosphotransferase system: evidence for direct binding of the glucose-specific enzyme III to the lactose permease. Proc Natl Acad Sci USA 1982; 79:1457–1461.Google Scholar
  65. 65.
    Dean DA, Reizer J, Nikaido H et al. Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phos-phoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclusion in proteoliposomes. J Biol Chem 1990; 265:21005–21010.Google Scholar
  66. 66.
    Nelson SO, Postma PW. Interactions in vivo between IIIGlc of the phosphoenol-pyruvate:sugar phosphotransferase system and the glycerol and maltose uptake systems of Salmonella typhimurium. Eur J Biochem 1984; 139:39–34.Google Scholar
  67. 67.
    De Boer M, Broekhuizen CP, Postma PW. Regulation of glycerol kinase by enzyme IIIGlc of the phosphoenolpyruvate:carabohydrate phosphotransferase system. J Bacteriol 1986; 167:393–395.Google Scholar
  68. 68.
    Scholte BJ, Schuitema ARJ, Postma PW. Characterization of factor IIIGlc in catabolite repression-resistant (err) mutants of Salmonella typhimurium. J Bacteriol 1982; 149:576–586.Google Scholar
  69. 69.
    Postma PW, Broekhuizen CP, Schuitema ARJ et al. Carbohydrate transport and metabolism in Escherichia coli and Salmonella typhimurium: regulation by the PEPxarbohydrate phosphotransferase system. In: Palmieri F, Quagliariello E, eds. Molecular basis of biomembrane transport. Amsterdam: Elsevier Science Publishers, 1988; 43–52.Google Scholar
  70. 70.
    Wilson TH, Yunker PL, Hansen CL. Lactose transport mutants of Escherichia coli resistant to inhibition by the phosphotransferase system. Biochim Biophys Acta 1990; 1029:113–116.Google Scholar
  71. 71.
    Kühnau S, Reyes M, Sievertsen M et al. The activities of the Escherichia coli MalK protein in maltose transport, regulation and inducer exclusion can be separated by mutations. J Bacteriol 1991; 174:2180–2186.Google Scholar
  72. 72.
    Kuroda M, De Waard S, Mizushima K et al. Resistance of the melibiose carrier to inhibition by the phosphotransferase system due to substitutions of amino acid residues in the carrier of Salmonella typhimurium. J Biol Chem 1992; 267:18336–18341.Google Scholar
  73. 73.
    Okada T, Ueyama K, Niiya S et al. Role of inducer exclusion in preferential utilization of glucose over melibiose in diauxie growth of Escherichia coli. J Bacteriol 1981; 146:1030–1037.Google Scholar
  74. 74.
    Postma PW, Van der Vlag J, De Waard JH et al. Enzymes II of the phosphotransferase system: transport and regulation. In: Torriani-Gorini AM, Yagil E, Silver S, eds. Phosphate in Microorganisms. Cellular and Molecular Biology. Washington: ASM Press, 1994; 169–174.Google Scholar
  75. 75.
    Zeng GQ, de Reuse H, Danchin A. Mutational analysis of the enzyme IIIGlc of the phosphoenolpyruvate phosphotransferase system in Escherichia coli. Res Microbiol 1993; 143:251–261.Google Scholar
  76. 76.
    Hurley JH, Worthylake D, Faber HR et al. Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Science 1993; 259:673–677.Google Scholar
  77. 77.
    Nelson SO, Schuitema ARJ, Postma PW. The phosphoenolpyruvate:glucose phospho-transferase system of Salmonella typhimurium. The phosphory-lated form of IIGlc. Eur J Biochem 1986; 154:337–341.Google Scholar
  78. 78.
    Cohn M, Horibata K. Physiology of the inhibition by glucose of the induced synthesis of the β-galactosidase-enzyme system of Escherichia coli. J Bacteriol 1959; 78:624–635.Google Scholar
  79. 79.
    Saier Jr MH. Novotny MJ, Comeau-Fuhrman D et al. 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 1983; 155:1351–1357.Google Scholar
  80. 80.
    Van der Vlag J, Van Dam K, Postma PW. Quantification of the regulation of glycerol and maltose metabolism by IIAGlc of the phosphoenolpyru-vate-dependent glucose phosphotransferase system in Salmonella typhimurium. J Bacteriol 1994; 176:3518–3526.Google Scholar
  81. 81.
    De Reuse H, Danchin A. The ptsH, ptsl and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex Operon with several modes of transcription. J Bacteriol 1988; 170: 3827–3837.Google Scholar
  82. 82.
    Fox DK, Presper KA, Adhya S et al. Evidence for two promoters upstream of the pts Operon: regulation by the cAMP receptor protein regulatory complex. Proc Natl Acad Sci USA 1992; 89:7056–7059.Google Scholar
  83. 83.
    Schnetz K, Rak B. ß-glucoside permease represses the bgl Operon of Escherichia coli by phosphorylation of the antiterminator protein and also interacts with glucose-specific enzyme III, the key element in catabolite control. Proc Natl Acad Sci USA 1990; 87:5074–5078.Google Scholar
  84. 84.
    Vogler AP, Broekhuizen CP, Schuitema A et al. Suppression of IIIGlc-defects by Enzymes IINag and IIBgl of the PEP: carbohydrate phosphotransferase system. Molec Microbiol 1988; 2:719–726.Google Scholar
  85. 85.
    Vogler AP, Lengeier JW. Complementation of a truncated membrane-bound Enzyme IINag from Klebsiella pneumoniae with a soluble Enzyme III in Escherichia coli K12. Mol Gen Genet 1988; 213:175–178.Google Scholar
  86. 86.
    Reizer J, Sutrina SL, Wu L-F et al. Functional interactions between proteins of the phosphoenolpyruvate:sugar phosphotransferase systems of Bacillus subtilis and Escherichia coli. J Biol Chem 1992; 267:9158–9169.Google Scholar
  87. 87.
    Levy S, Zeng G-Q, Danchin A. Cyclic AMP synthesis in Escherichia coli strains bearing known deletions in the pts phosphotransferase Operon. Gene 1990; 86:27–33.Google Scholar
  88. 88.
    Steinmetz M. Carbohydrate catabolism: pathways, enzymes, genetic regulation, and evolution. In: Sonenshein AL, Hoch JA, Losick R, eds. Bacillus subtilis and other gram-positive bacteria. Washington, DC: ASM 1993; 157–170.Google Scholar
  89. 89.
    Kjellberg S. Starvation in Bacteria. New York & London:Plenum Press, 1993.Google Scholar
  90. 90.
    Chuang, S, Daniels DL, Blattner FR. Global regulation of gene expression in Escherichia coli. J Bacteriol 1993;175:2026–2036.Google Scholar
  91. 91.
    Jahreis K, Postma PW, Lengeler JW. Nucleotide sequence of the ilvH-fruR gene region of Escherichia coli K12 and Salmonella typhimurium LT2. Mol Gen Genet 1991; 226:332–336.Google Scholar
  92. 92.
    Vartak NB, Reizer J, Reizer A et al. Sequence and evolution of the FruR protein of Salmonella typhimurium’. a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res Microbiol 1991; 142:951–963.Google Scholar
  93. 93.
    Jahreis K, Lengeler JW. Molecular analysis of two ScrR repressors and of a ScrR-FruR hybrid repressor for sucrose and D-fructose specific regulons from enteric bacteria. Molec Microbiol 1993; 9:195–209.Google Scholar
  94. 94.
    Geerse RH, Ruig, CR, Schuitema ARJ et al. Relationship between pseudo-HPr and the PEP: fructose phosphotransferase system in Salmonella typhimurium and Escherichia coli. Mol Gen Genet 1986; 203:435–444.Google Scholar
  95. 95.
    Kornberg HL, Elvin CM. Location and function of fruC, a gene involved in the regulation of fructose utilization by Escherichia coli. J Gen Microbiol 1987; 133:341–346.Google Scholar
  96. 96.
    Reiner AM. Xylitol and D-arabitol toxicities due to derepressed fructose, galactitol and sorbitol phosphotransferases of Escherichia coli. J Bacteriol 1977; 132:166–173.Google Scholar
  97. 97.
    Geerse RH, Izzo F, Postma PW. The PEP:fructose phosphotransferase system in Salmonella typhimurium: FPr combines Enzyme IIIFru and pseudo-HPr activities. Mol Gen Genet 1989; 216:517–525.Google Scholar
  98. 98.
    Ramseier TM, Nègre D, Cortay J-C et al. In vitro binding of the pleiotropic transcriptional regulatory protein, FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and Salmonella typhimurium. J Mol Biol 1993; 234:28–44.Google Scholar
  99. 99.
    Chin AM, Feldheim DA, Saier Jr MH. Altered transcriptional patterns affecting several metabolic pathways in strains of Salmonella typhimurium which overexpress the fructose regulon. J Bacteriol 1989; 171:2424–2434.Google Scholar
  100. 100.
    Chin AM, Feucht BU, Saier MH Jr. Evidence for regulation of gluconeo-genesis by the fructose phosphotransferase system in Salmonella typhimurium. J Bacteriol 1987; 169:897–899.Google Scholar
  101. 101.
    Geerse RH, van der Pluijm J, Postma PW. The repressor of the PEP: fructose phosphotransferase system is required for the transcription of the pps gene of Escherichia coli. Mol Gen Genet 1989; 218:348–352.Google Scholar
  102. 102.
    Cortay JC, Nègre D, Scarabel M et al. In vitro asymmetric binding of the pleiotropic regulatory protein FruR, to the ace operator controlling glyoxylate shunt enzyme synthesis. J Biol Chem 1994; 269: 14885–14891.Google Scholar
  103. 103.
    Fox DK, Meadow ND, Roseman S. Phosphate transfer between acetate kinase and enzyme I of the bacterial phosphotransferase system. J Biol Chem 1986; 261:13498–13503.Google Scholar
  104. 104.
    McCleary WR, Stock JB, Ninfa AJ. Is acetyl phosphate a global signal in Escherichia coli? J Bacteriol 1993; 175:2793–2798.Google Scholar
  105. 105.
    Jones DHA, Franklin FCH, Thomas CM. Molecular analysis of the Operon which encodes the RNA polymerase sigma factor σ54 of Escherichia coli. Microbiology 1994; 140:1035–1043.Google Scholar
  106. 106.
    Reizer J, Reizer A, Saier Jr MH et al. A proposed link between nitrogen and carbon metabolism involving protein phosphorylation in bacteria. Protein Sci 1992; 1:722–726.Google Scholar
  107. 107.
    Merrick MJ, Coppard JR. Mutations in genes downstream of the rpoN gene (encoding a54) of Klebsiella pneumoniae affect expression from σ54-dependent promoters. Molec Microbiol 1989; 3:1765–1775.Google Scholar
  108. 108.
    Begley GS, Jacobson GR. Overexpression, phosphorylation, and growth effects of ORF162, a Klebsiella pneumoniae protein that is encoded by a gene linked to rpoN, a gene encoding σ54. FEMS Microbiol Lett 1994; 119: 389–394.Google Scholar
  109. 109.
    Powell BS, Court DL, Inada T et al. Novel proteins of the phosphotransferase system encoded within the rpoN Operon of Escherichia coli. Enzyme IIAntr affects growth on organic nitrogen and the conditional lethality of an era(Ts) mutant. J Biol Chem 1995; 270:4822–4839.Google Scholar
  110. 110.
    Van der Vlag J, van ’t Hof R, Van Dam K et al. Control of glucose metabolism by the enzymes of the glucose phosphotransferase system in Salmonella typhimurium. Eur J Biochem 1995; 230:170–182.Google Scholar
  111. 111.
    Hubbard MJ, Cohen P. On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem Sci 1993; 18:172–177.Google Scholar
  112. 112.
    Alex LA, Simon MI. Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. Trends Genet 1994; 10:133–138.Google Scholar

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  • Joseph W. Lengeler

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