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Regulation of Aerobic and Anaerobic Metabolism by the Arc system

  • A. Simon Lynch
  • Edmund C. C. Lin

Abstract

During the course of the evolution of microbial bioenergetics, progenitors of E. coli probably acquired in a stepwise temporal fashion metabolic pathways for fermentation, anaerobic respiration, and aerobic respiration for the process of energy transduction.1,2 The acquisition of these different pathways, combined with the apparent development of successive layers of regulatory mechanisms to control them, enables E. coli to exploit adroitly environmental energy sources to their greatest possible advantage. To this end, a key strategy is to channel electrons from donors to terminal acceptors such that the overall potential difference is maximized for any given growth condition. Conspicuous consequences are improved growth rate and/or yield for any given carbon and energy source.

Keywords

Escherichia Coli Anaerobic Metabolism Receiver Domain Phosphoryl Group Acetyl Phosphate 
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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References

  1. 1.
    Gest H. The evolution of biological energy-transducing systems. FEMS Microbiol Lett 1980; 7:70–77.Google Scholar
  2. 2.
    Wilson TH, Lin ECC. Evolution of membrane bioenergetics. J Supramol Structure 1980; 13:421–446.Google Scholar
  3. 3.
    Hirsch CA, Rasminsky M, Davis BD et al. A fumarate reductase in Escherichia coli distinct from succinate dehydrogenase. J Biol Chem 1963; 238:3770–3774.Google Scholar
  4. 4.
    Amarasingham CR, Davis BJ. Regulation of α-ketoglutarate dehydrogenase formation in Escherichia coli. J Biol Chem 1965; 240:3664–3668.Google Scholar
  5. 5.
    Gray CT, Wimpenny JWT, Hughes DE et al. Regulation of metabolism in facultative bacteria. 1. Structural and functional changes in Escherichia coli associated with shifts between the aerobic and anaerobic states. Biochim Biophys Acta 1966; 117:22–32.Google Scholar
  6. 6.
    Gray CT, Wimpenny JWT, Mossman MR. Regulation of metabolism in facultative bacteria. II. Effects of aerobiosis, anaerobiosis and nutrition on the formation of Krebs cycle enzymes in Escherichia coli. Biochim Biophys Acta 1966; 117:33–41.Google Scholar
  7. 7.
    Hino S, Maeda M. Effect of oxygen on the development of respiratory activity in Escherichia coli. J Gen Appl Microbiol 1966; 12:247–265.Google Scholar
  8. 8.
    Cavari BZ, Avi-Dor Y, Grossowicz N. Induction by oxygen of respiration and phosphorylation of anaerobically grown Escherichia coli. J Bacteriol 1968; 96:751–759.Google Scholar
  9. 9.
    Smith MW, Neidhardt FC. Proteins induced by aerobiosis in Escherichia coli. J Bacteriol 1983; 154:344–350.Google Scholar
  10. 10.
    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
  11. 11.
    Iuchi S, Cameron DC, Lin ECC. A second global regulator gene (arcB) mediating repression of enzymes in aerobic pathways of Escherichia coli. J Bacteriol 1989; 171:868–873.Google Scholar
  12. 12.
    Buxton RS, Drury LS. Cloning and insertional inactivation of the dye (sfraA) gene, mutation of which affects sex factor F expression and dye sensitivity of Escherichia coli K12. J Bacteriol 1983; 154:1309–1314.Google Scholar
  13. 13.
    Buxton RS, Drury LS, Curtis CAM. Dye sensitivity correlated with envelope protein changes in dye (sfraA) mutants of Escherichia coli K12 defective in the expression of the sex factor F. J Gen Microbiol 1983; 129:3363–3370.Google Scholar
  14. 14.
    Buxton RS, Drury LS. Identification of the dye gene product, mutational loss of which alters envelope protein composition and also affects sex factor F expression in Escherichia coli K-12. Mol Gen Genet 1984; 194:241–247.Google Scholar
  15. 15.
    Buxton RS, Hammer-Jespersen K, Hansen TD. Insertion of bacteriophage lambda into the deo operon of Escherichia coli K-12 and isolation of plaque-forming lambda deo + transducing bacteriophages. J Bacteriol 1978; 136:668–681.Google Scholar
  16. 16.
    Roeder W, Somerville RL. Cloning the trpR gene. Mol Gen Genet 1978; 176:361–368.Google Scholar
  17. 17.
    Lerner T, Zinder N. Chromosomal regulation of sexual expression in Escherichia coli. J Bacteriol 1979; 137:1063–1065.Google Scholar
  18. 18.
    Beutin L, Achtman M. Two Escherichia coli chromosomal cistrons, sfrA and sfrB, which are needed for expression of F factor tra functions. J Bacteriol 1979; 139:730–737.Google Scholar
  19. 19.
    Beutin L, Manning P, Achtman M et al. sfrA and sfrB products of Escherichia coli K-12 are transcription control factors. J Bacteriol 1981; 145:840–844.Google Scholar
  20. 20.
    McEwen J, Silverman P. Chromosomal mutations of Escherichia coli that alter expression of conjugative plasmid functions. Proc Natl Acad Sci USA 1980; 77:513–517.Google Scholar
  21. 21.
    Silverman P, Nat K, McEwen J et al. Selection of Escherichia coli K-12 chromosomal mutants that prevent expression of F-plasmid functions. J Bacteriol 1980; 143:1519–1523.Google Scholar
  22. 22.
    Ezaki B, Ogura T, Mori H et al. Involvement of DnaK protein in mini-F plasmid replication: temperature-sensitive seg mutations are located in the dnaK gene. Mol Gen Genet 1989; 218:183–189.Google Scholar
  23. 23.
    Drury LS, Buxton RS. DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the Dye and OmpR proteins. J Biol Chem 1985; 260:4236–4242.Google Scholar
  24. 24.
    Ronson CW, Nixon BT, Ausubel FM. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell 1987; 49:579–581.Google Scholar
  25. 25.
    Parkinson JS, Kofoid EC. Communication modules in bacterial signaling proteins. Ann Rev Genet 1992; 26:71–112.Google Scholar
  26. 26.
    Volz K. Structural conservation in the CheY superfamily. Biochemistry 1993; 32:11741–11753.Google Scholar
  27. 27.
    Alex LA, Simon MI. Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. Trends Biochem Sci 1994; 10:133–139.Google Scholar
  28. 28.
    Pao GM, Tarn R, Lipschitz LS et al. Response regulators: structure, function and evolution. Res Microbiol 1994; 145:356–362.Google Scholar
  29. 29.
    Swanson RV, Alex LA, Simon MI. Histidine and aspartate phosphorylation: two-component systems and the limits of homology. Trends Biochem Sci 1994; 19:485–490.Google Scholar
  30. 30.
    Stock JB, Surette MG, Levit M et al. Two-component signal transduction systems: structure-function relationships and mechanisms of catalysis. In: Hoch JA, Silhavy TJ, eds. Two-component signal transduction. Washington: ASM Press, 1995:25–52.Google Scholar
  31. 31.
    Volz K. Structural and functional conservation in response regulators. In: Hoch JA, Silhavy TJ, eds. Two-component signal transduction. Washington: ASM Press, 1995:53–64.Google Scholar
  32. 32.
    Stock AM, Mottonen JM, Stock JB et al. Three-dimensional structure of CheY, the response regulator of bacterial Chemotaxis. Nature 1989; 337:745–749.Google Scholar
  33. 33.
    Volz K, Matsumura P. Crystal structure of Escherichia coli Che Y refined at 1.7 A resolution. J Biol Chem 1991; 266:15511–15519.Google Scholar
  34. 34.
    Bourret RB, Drake SK, Chervitz SA et al. Activation of the phosphosignaling protein Che Y. II. Analysis of the activated mutants by 19F NMR and protein engineering. J Biol Chem 1993; 268:13089–13096.Google Scholar
  35. 35.
    Bruix M, Pascual J, Santoro J et al. 1H- and 15-N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein. Eur J Biochem 1993; 215:573–585.Google Scholar
  36. 36.
    Drake SK, Bourret RB, Luck LA et al. Activation of the phosphosignaling protein Che Y. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering. J Biol Chem 1993; 268:13081–13088.Google Scholar
  37. 37.
    Stock AM, Martinez-Hackert E, Rasmussen BF et al. Structure of the Mg2−-bound form of CheY and mechanism of phosphoryl transfer in bacterial Chemotaxis. Biochemistry 1993; 32:13375–13380.Google Scholar
  38. 38.
    Compan I, Touati D. Anaerobic activation of arcA transcription in Escherichia coli: roles of Fnr and ArcA. Mol Microbiol 1994; 11:955–964.Google Scholar
  39. 39.
    Park SJ, Cotter PA, Gunsalus RP. Autoregulation of the arcA gene of Escherichia coli. Am Soc Microbiol Abstr 1992; 92:207(Abstract)Google Scholar
  40. 40.
    Slauch JM, Garrett S, Jackson DE et al. EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12. J Bacteriol 1988; 170:439–441.Google Scholar
  41. 41.
    Iuchi S, Matsuda Z, Fujiwara T et al. The arcB gene of Escherichia coli encodes a sensor-regulator protein for anaerobic repression of the arc modulon. Mol Microbiol 1990; 4:715–727.Google Scholar
  42. 42.
    Stout V, Gottesman S. RcsB and RcsC: a two-component regulator of capsule synthesis in Escherichia coli. J Bacteriol 1990; 172:659–669.Google Scholar
  43. 43.
    Nagasawa S, Ishige K, Mizuno T. Novel members of the two-component signal transduction genes in Escherichia coli. J Biochem 1993; 114:350–357.Google Scholar
  44. 44.
    Ishige K, Nagasawa S, Tokishita S-I et al. A novel device of bacterial signal transducers. EMBO J 1994; 13:5195–5202.Google Scholar
  45. 45.
    Uhl MA, Miller JF. Autophosphorylation and phosphotransfer in the Bordetella pertussis BvgAS signal transduction cascade. Proc Natl Acad Sci USA 1994; 91:1163–1167.Google Scholar
  46. 46.
    Uhl MA, Miller JF. Bordetella pertussis BvgAS virulence control system. In: Hoch JA, Silhavy TJ, eds. Two-component signal transduction. Washington: ASM Press, 1995:333–350.Google Scholar
  47. 47.
    Iuchi S, Lin ECC. Mutational analysis of signal transduction by ArcB: a membrane sensor protein for anaerobic expression of operons involved in the central aerobic pathways in Escherichia coli. J Bacteriol 1992; 174:3972–3980.Google Scholar
  48. 48.
    Iuchi S, Lin ECC. Purification and phosphorylation of the Arc regulatory components of Escherichia coli. J Bacteriol 1992; 174:5617–5623.Google Scholar
  49. 49.
    Iuchi S. Phosphorylation/dephosphorylation of the receiver module at the conserved aspartate residue controls transphosphorylation activity of histidine kinase in sensor protein ArcB of Escherichia coli. J Biol Chem 1993; 263:23972–23980.Google Scholar
  50. 50.
    Yang Y, Inouye M. Intermolecular complementation between two defective mutant signal-transducing receptors of Escherichia coli. Proc Natl Acad Sci USA 1991; 88:11057–11061.Google Scholar
  51. 51.
    Lin ECC, Iuchi S. Role of protein phosphorylation in the regulation of aerobic metabolism by the Arc system in Escherichia coli. In: TorrianiGorini A, Yagil E, Silver S, eds. Phosphate in microorganisms: cellular and molecular biology. Washington, D.C.: American Society for Microbiology, 1994:290–295.Google Scholar
  52. 52.
    Silverman P. Host cell-plasmid interactions in the expression of DNA donor activity by F+ strains of Escherichia coli K-12. Bioassays 1985; 2:254–259.Google Scholar
  53. 53.
    Albin R, Weber R, Silverman PM. The Cpx proteins of Escherichia coli K12: immunologic detection of the chromosomal cpxA gene product. J Biol Chem 1986; 261:4698–4705.Google Scholar
  54. 54.
    Silverman P, Wichersham E, Harris R. Regulation of the F plasmid traY promoter by host and plasmid factors. J Mol Biol 1991; 218:119–128.Google Scholar
  55. 55.
    Gaudin H, Silverman P. Contributions of promoter context and structure to regulated expression of the F plasmid traY promoter in Escherichia coli K12. Mol Microbiol 1993; 8:335–342.Google Scholar
  56. 56.
    Iuchi S, Furlong D, Lin ECC. Differentiation of arcA, arcB, and cpxA mutant phenotypes of Escherichia coli by sex pilus formation and enzyme regulation. J Bacteriol 1989; 171:2889–2893.Google Scholar
  57. 57.
    Silverman PM, Tran L, Harris R et al. Accumulation of the F plasmid TraJ protein in cpx mutants of Escherichia coli. J Bacteriol 1993; 175:921–925.Google Scholar
  58. 58.
    Dong J-M, Iuchi S, Kwan H-S et al. The deduced amino acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli. Gene 1993; 136:227–230.Google Scholar
  59. 59.
    Plunkett G, Burland V, Daniels DL et al. Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nuc Acids Res 1993; 21:3391–3398.Google Scholar
  60. 60.
    Danese PN, Snyder WB, Cosma CL et al. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes & Development 1995;9:387–398.Google Scholar
  61. 61.
    Snyder WB, Davis LJB, Danese PN et al. Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway. J Bacteriol 1995; 177:4216–4223.Google Scholar
  62. 62.
    Neidhardt FC, Ingraham JL, Schaechter M. Physiology of the bacterial cell. A molecular approach. Sinauer Associates, Inc. Sunderland, MA: 1990. pp. 382–383.Google Scholar
  63. 63.
    Gunsalus RP. Control of electron flow in Escherichia coli: coordinated transcription of respiratory pathway genes. J Bacteriol 1992; 174: 7069–7074.Google Scholar
  64. 64.
    Guest JR, Russell GC. Complexes and complexities of the citric acid cycle in Escherichia coli. Curr Topics Cell Reg 1992; 33:231–247.Google Scholar
  65. 65.
    Iuchi S, Lin ECC. Adaptation of Escherichia coli to respiratory conditions: regulation of gene expression. Cell 1991; 66:5–7.Google Scholar
  66. 66.
    Iuchi S, Lin ECC. Adaptation of Escherichia coli to redox environments by gene expression. Mol Microbiol 1993; 9:9–15.Google Scholar
  67. 67.
    Gunsalus RP, Park S-J. Aerobic-anaerobic gene regulation in Escherichia coli control by the ArcAB and Fnr regulons. Res Microbiol 1994; 145:437–450.Google Scholar
  68. 68.
    Andersson DI, Roth JR. Redox regulation of the genes for cobinamide biosynthesis in Salmonella typhimurium. J Bacteriol 1989; 171:6734–6739.Google Scholar
  69. 69.
    Andersson DL Involvement of the Arc system in redox regulation of the Cob Operon in Salmonella typhimurium. Mol Microbiol 1992; 6: 1491–1494.Google Scholar
  70. 70.
    Ailion M, Bobik TA, Roth JR. Two global regulatory systems (Crp and Arc) control the cobalamin/propanediol regulon of Salmonella typhimurium. J Bacteriol 1993; 175:7200–7208.Google Scholar
  71. 71.
    Wall D, Delaney JM, Fayet O et al. arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d Operon. J Bacteriol 1992; 174:6554–6562.Google Scholar
  72. 72.
    Frey B, Janel G, Michelson U et al. Mutations in the Escherichia coli fnr and tgt genes: control of molybdate reductase activity and the cytochrome d complex by fnr. J Bacteriol 1989; 171:1524–1530.Google Scholar
  73. 73.
    Cotter PA, Chepuri V, Gennis RB et al. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the for gene product. J Bacteriol 1990; 172:6333–6338.Google Scholar
  74. 74.
    Iuchi S, Chepuri V, Fu H-A et al. Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: study utilizing deletions and lac fusions of cyo and cyd. J Bacteriol 1990; 172:6020–6025.Google Scholar
  75. 75.
    Fu H-A, Iuchi S, Lin ECC. The requirement of ArcA and Fnr for peak expression of the cyd Operon in Escherichia coli under microaerobic conditions. Mol Gen Genet 1991; 226:209–213.Google Scholar
  76. 76.
    Bogachev AV, Murtazina RA, Skulachev VP. Cytochrome d induction in Escherichia coli growing under unfavorable conditions. FEBS Lett 1993; 336:75–78.Google Scholar
  77. 77.
    Cotter PA, Gunsalus RP. Contribution of the fnr and arcA gene products in coordinate regulation of cytochrome o and d oxidase (cyoABCDE and cydAB) genes in Escherichia coli. FEMS Microbiol Lett 1992; 91:31–36.Google Scholar
  78. 78.
    Georgiou CD, Dueweke TJ, Gennis RB. Regulation of expression of the cytochrome d terminal oxidase in Escherichia coli. J Bacteriol 1988; 170:961–966.Google Scholar
  79. 79.
    Fang H, Gennis RB. Identification of the transcriptional start site of the cyd Operon from Escherichia coli. FEMS Microbiol Lett 1993; 108:237–242.Google Scholar
  80. 80.
    Berg BL, Stewart V. Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics 1990; 125:691–702.Google Scholar
  81. 81.
    Birkmann A, Zinoni F, Sawers G et al. Factors affecting transcriptional regulation of the formate-hydrogen-lyase pathways of Escherichia coli. Arch Microbiol 1987; 148:44–51.Google Scholar
  82. 82.
    Li J, Stewart V. Localization of upstream sequence elements required for nitrate and anaerobic induction of fdn (formate dehydrogenase-N) Operon expression in Escherichia coli K-12. J Bacteriol 1992; 174:4935–4942.Google Scholar
  83. 83.
    Sawers G, Böck A. Anaerobic regulation of pyruvate formate-lyase from Escherichia coli K-12. J Bacteriol 1988; 170:5330–5336.Google Scholar
  84. 84.
    Wong KK, Suen KL, Kwan HS. Transcription of pfl is regulated by anaero-biosis, catabolite repression, pyruvate, and oxrA: pfl::Mu dA Operon fusions of Salmonella typhimurium. J Bacteriol 1989; 171:4900–4905.Google Scholar
  85. 85.
    Sawers G. Specific transcriptional requirements for positive regulation of the anaerobically inducible pfl Operon by ArcA and FNR. Mol Microbiol 1993; 10:737–747.Google Scholar
  86. 86.
    Sawers G, Suppmann B. Anaerobic induction of pyruvate formate-lyase gene expression is mediated by the ArcA and FNR proteins. J Bacteriol 1992; 174:3474–3478.Google Scholar
  87. 87.
    Sirko A, Zehelein E, Freundlich M et al. Integration host factor is required for anaerobic pyruvate induction of pfl Operon expression in Escherichia coli. J Bacteriol 1993; 175:5769–5777.Google Scholar
  88. 88.
    Drapai N, Sawers G. Purification of ArcA and analysis of its specific interaction with the pfl promoter-regulatory region. Mol Microbiol 1995; 16:597–607.Google Scholar
  89. 89.
    Kaiser M, Sawers G. Nitrate repression of the Escherichia coli pfl Operon is mediated by the dual sensors NarQ and NarX and the dual regulators NarL and NarP. J Bacteriol 1995; 177:3647–3655.Google Scholar
  90. 90.
    Woods SA, Guest JR. Differential roles of the Escherichia coli fumarases and fnr-dependent expression of fumarase B and aspartase. FEMS Microbiol Lett 1987; 48:219–224.Google Scholar
  91. 91.
    Iuchi S, Cole ST, Lin ECC. Multiple regulatory elements for the glpA Operon encoding anaerobic glycerol-3-phosphate dehydrogenase and the glpD operon encoding aerobic glycerol-3-phosphate dehydrogenase in Escherichia coli: further characterization of respiratory control. J Bacteriol 1990; 172:179–184.Google Scholar
  92. 92.
    Park S-J, McCabe J, Turna J et al. Regulation of the citrate synthase (gltA) gene of Escherichia coli in response to anaerobiosis and carbon supply: role of the arcA gene product. J Bacteriol 1994; 176:5086–5092.Google Scholar
  93. 93.
    Darie LS, Gunsalus RP. Effect of heme and oxygen availability on hemA gene expression in Escherichia coli: role of the fnr, arcA, and himA gene products. J Bacteriol 1994; 176:5270–5276.Google Scholar
  94. 94.
    Jamieson DJ, Sawers RG, Rugman PA et al. Effects of anaerobic regulatory mutations and catabolite repression on regulation of hydrogen metabolism and hydrogenase isoenzyme composition in Salmonella typhimurium. J Bacteriol 1986; 168:405–411.Google Scholar
  95. 95.
    Sawers RG, Ballantine SP, Boxer DH. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J Bacteriol 1985; 164:1324–1331.Google Scholar
  96. 96.
    Jamieson DJ, Higgins CF. Two genetically distinct pathways for transcriptional regulation of anaerobic gene expression in Salmonella typhimurium. J Bacteriol 1986; 168:389–397.Google Scholar
  97. 97.
    Brondsted L, Atlung T. Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli. J Bacteriol 1994; 176:5423–5428.Google Scholar
  98. 98.
    Iuchi S, Aristarkhov A, Dong J-M et al. Effects of nitrate respiration on expression of the Arc-controlled operons encoding succinate dehydrogenase and flavin-linked L-lactate dehydrogenase. J Bacteriol 1994; 176:1695–1701.Google Scholar
  99. 99.
    Dong J-M, Taylor JS, Latour DJ et al. Three overlapping lct genes involved in L-lactate utilization by Escherichia coli. J Bacteriol 1993; 175:6671–6678.Google Scholar
  100. 100.
    Bongaerts J, Zoske S, Weidner U et al. Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors and gene regulators. Mol Microbiol 1995; 16:521–534.Google Scholar
  101. 101.
    Quail MA, Haydon DJ, Guest JR. The pdhR-aceEF-lpd operon of Escherichia coli expresses the pyruvate dehydrogenase complex. Mol Microbiol 1994; 12:95–104.Google Scholar
  102. 102.
    Park S-J, Tseng C-P, Gunsalus RP. Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr. Mol Microbiol 1995; 15:473–482.Google Scholar
  103. 103.
    Tardat B, Touati D. Two global regulators repress the anaerobic expression of MnSOD in Escherichia coli: Fur (ferric uptake regulation) and Arc (aerobic respiration control). Mol Microbiol 1991; 5:455–465.Google Scholar
  104. 104.
    Tardat B, Touati D. Iron and oxygen regulation of Escherichia coli MnSOD expression: competition between the global regulators Fur and ArcA for binding to DNA. Mol Microbiol 1993; 9:53–63.Google Scholar
  105. 105.
    Hassan HM, Sun HC. Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli. Proc Natl Acad Sci USA 1992; 89:3217–3221.Google Scholar
  106. 106.
    Compan I, Touati D. Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12. J Bacteriol 1993; 175:1687–1696.Google Scholar
  107. 107.
    Privalle CT, Kong SE, Fridovich I. Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation. Proc Natl Acad Sci USA 1993; 90:2310–2314.Google Scholar
  108. 108.
    Beaumont MD, Hassan HM. Characterization of regulatory mutations causing anaerobic derepression of the sodA gene in Escherichia coli K12: cooperation between cis- and trans-acting regulatory loci. J Gen Microbiol 1993; 139:2677–2684.Google Scholar
  109. 109.
    Silverman PM, Rother S, Gaudin H. Arc and Sfr functions of the Escherichia coli K-12 arcA gene product are genetically and physiologically separable. J Bacteriol 1991; 173:5648–5652.Google Scholar
  110. 110.
    Silverman PM, Wickersham E, Rainwater S et al. Regulation of the F-plasmid traY promoter in Escherichia coli K12 as a function of sequence context. J Mol Biol 1991; 220:271–279.Google Scholar
  111. 111.
    Cotter PA, Darie S, Gunsalus RP. The effect of iron limitation on expression of the aerobic and anaerobic electron transport pathways genes in Escherichia coli. FEMS Microbiol Lett 1992; 79:227–232.Google Scholar
  112. 112.
    Stewart V. Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli. Mol Microbiol 1993; 9:425–434.Google Scholar
  113. 113.
    Tyson KL, Bell AI, Cole JA et al. Definition of nitrite and nitrate response elements at the anaerobically inducible Escherichia coli nirB promoter: interactions between FNR and NarL. Mol Microbiol 1993; 7:151–157.Google Scholar
  114. 114.
    Li J, Kustu S, Stewart V. In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA Operon control regions of Escherichia coli K-12. J Mol Biol 1994; 241:150–165.Google Scholar
  115. 115.
    Walker MS, DeMoss JA. NarL-phosphate must bind to multiple upstream sites to activate transcription from the narG promoter of Escherichia coli. Mol Microbiol 1994; 633:641Google Scholar
  116. 116.
    Tyson KL, Cole JA, Busby SJW. Nitrite and nitrate regulation at the promoters of two Escherichia coli operons encoding nitrite reductase: identification of common target heptamers for both NarP- and NarL- dependent regulation. Mol Microbiol 1994; 13:1045–1055.Google Scholar
  117. 117.
    Wanner BL. Is cross regulation by phosphorylation of two-component response regulator proteins important in bacteria? J Bacteriol 1992; 174:2053–2058.Google Scholar
  118. 118.
    McCleary WR, Stock JB, Ninfa AJ. Is acetyl phosphate a global signal in Escherichia col?. J Bacteriol 1993; 175:2793–2798.Google Scholar
  119. 119.
    McCleary WR, Stock JB. Acetyl phosphate and the activation of two-component response regulators. J Biol Chem 1994; 269:31567–31572.Google Scholar
  120. 120.
    Aiba H, Mizuno T, Mizushima S. Transfer of phosphoryl group between two regulatory proteins involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli. J Biol Chem 1989; 264:8563–8567.Google Scholar
  121. 121.
    Nakashima K, Kanamuru K, Aiba H et al. Signal transduction and osmoregulation in Escherichia coli. J Biol Chem 1991; 266:10775–10780.Google Scholar
  122. 122.
    Holman TR, Wu Z, Wanner BL et al. Identification of the DNA-binding site for the phospshorylated VanR protein required for vancomycin resistance in Enterococcus faecium. Biochemistry 1994; 33:4625–4631.Google Scholar
  123. 123.
    Nystrom T. The glucose-starvation stimulon of Escherichia coli induced and repressed synthesis of enzymes of central metabolic pathways and role for acetyl phosphate in gene expression and starvation survival. Mol Microbiol 1994; 12:833–843.Google Scholar
  124. 124.
    Poole RK, Ingledew WJ. The pathways of electrons to oxygen. In: Neidhardt FC, Ingraham JL, Low KB et al. Escherichia coli and Salmonella typhimurium: cellular and molecular biology. Washington, D.C. American Society for Microbiology, 1987:170–200.Google Scholar
  125. 125.
    Wissenbach U, Ternes D, Unden G. An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration. Arch Microbiol 1992; 158:68–73.Google Scholar
  126. 126.
    Wallace BJ, Young IG. Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA menA double quinone mutant. Biochim Biophys Acta 1977; 461:84–100.Google Scholar
  127. 127.
    Iuchi S, Lin ECC. Signal transduction in the Arc system for control of operons encoding aerobic respiratory enzymes. In: Hoch JA, Silhavy TJ, eds. Two-component signal transduction. Washington: ASM Press, 1995:223–232.Google Scholar

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© R.G. Landes Company 1996

Authors and Affiliations

  • A. Simon Lynch
  • Edmund C. C. Lin

There are no affiliations available

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