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1992-11-01
2021-05-14
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References

  1. Amarasingham C. D., Davis B. D. 1965; Regulation of α-ketoglutarate dehydrogenase formation in Escherichia coli. Journal of Biological Chemistry 240:3664–3668
    [Google Scholar]
  2. Bell A. I., Gaston K. L., Busby S. J. W. 1989a; Cloning of binding sequences for the Escherichia coli transcriptional activators FNR and CRP, location of bases involved in discrimination between FNR and CRP. Nucleic Acids Research 17:3865–3874
    [Google Scholar]
  3. Bell P. J., Andrews S. C., Sivak M. N., Guest J.R. 1989b Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of Escherichia coli K-12. Journal of Bacteriology 171:3494–3503
    [Google Scholar]
  4. Drury L. S., Buxton R. S. 1985; DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the Dye and OmpR proteins. Journal of Biological Chemistry 260:4236–4242
    [Google Scholar]
  5. Gray C. T., Wimpenny J. W. T., Mossman M. R. 1966; Regulation of metabolism in facultative bacteria. II. Effects of aerobiosis, anaerobiosis and nutrition on the formation of Krebs cycle enzymes in Escherichia coli. Biochimica et Biophysica Acta 117:33–41
    [Google Scholar]
  6. Green J., Trageser M., Six S., Unden G., Guest J. R. 1991; Characterization of the FNR protein of Escherichia coli, an ironbinding transcriptional regulator. Proceedings of the Royal Society of London B244137–144
    [Google Scholar]
  7. Hentze M. W., Argos P. 1991; Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase. Nucleic Acids Research 19:1739–1740
    [Google Scholar]
  8. Luchi S., Lin E. C. C. 1988; Arca (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways. Proceedings of the National Academy of Sciences of the United States of America 851888–1892
    [Google Scholar]
  9. Luchi S., Matsuda Z., Fujiwara T., Lin E. C. C. 1990; The arcB gene of Escherichia coli encodes a sensor-regulator protein for anaerobic repression of the arc modulon. Molecular Microbiology 4:715–727
    [Google Scholar]
  10. Kaptain S., Downey W. E., Tang C., Philpott C., Haile O., Orloff D. G., Harford J.B., Rouault T. A., Klausner R. D. 1991; A regulated RNA binding protein also possesses aconitase activity. Proceedings of the National Academy of Sciences of the United States of America 8810109–10113
    [Google Scholar]
  11. Kiley P. J., Reznikoff W. S. 1991; Fnrmutants that activate gene expression in the presence of oxygen. Journal of Bacteriology 173:16–22
    [Google Scholar]
  12. Lin E. C. C., Iuchi S. 1991; Regulation of gene expression in fermentative and respiratory systems in Escherichia coli and related bacteria. Annual Review of Genetics 25:361–387
    [Google Scholar]
  13. Liochev S. I., Fridovich I. 1992; Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proceedings of the National Academy of Sciences of the United States of America 895892–5896
    [Google Scholar]
  14. Prodromou C., Haynes M. J., Guest J. R. 1991; Theaconitaseof Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn). Journal of General Microbiology 137:2505–2515
    [Google Scholar]
  15. Prodromou C., Artymiuk P. J., Guest J. R. 1992; The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases. European Journal of Biochemistry 204:599–609
    [Google Scholar]
  16. Robbins A. H., Stout C. D. 1989; The structure of aconitase. Proteins 5:289–312
    [Google Scholar]
  17. Rouault T. A., Stout C. D., Kaptain S., Harford J. B., Klausner R. D. 1991; Structural relationship between an ironregulated RNA-binding protein (IRE-BP) and aconitase: functional implications. Cell 64:881–883
    [Google Scholar]
  18. Sharrocks A. D., Green J., GUEST J. R. 1991; FNR activates and represses transcription in vitro. Proceedings of the Royal Society of London B245219–226
    [Google Scholar]
  19. Shaw D. J., Rice D. W., Guest J. R. 1983; Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli. Journal of Molecular Biology 166:241–247
    [Google Scholar]
  20. Spencer M. E., Guest J. R. 1985; Transcription analysis of the sucAB, aceEF and !pd genes of Escherichia coli. Molecular and General Genetics 200:145–154
    [Google Scholar]
  21. Spiro S., Guest J. R. 1987; Activation of the lac operon of Escherichia coli by a mutant FNR protein. Molecular Microbiology 1:553–558
    [Google Scholar]
  22. Spiro S., Guest J. R. 1990; FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiology Reviews 15:399–428
    [Google Scholar]
  23. Spiro S., Guest J. R. 1991; Adaptive responses to oxygen limitation in Escherichia coli. Trends in Biochemical Sciences 16:310–314
    [Google Scholar]
  24. Spiro S., Gaston K. L., Bell A. I., Roberts R. E., Busby S. J. W., Guest J. R. 1990; Interconversion of the DNA-binding specificities of two related transcription regulators, CRP and FNR. Molecular Microbiology 4:1831–1838
    [Google Scholar]
  25. Stephenson M. 1949 Bacterial Metabolism,, 3rd edn. London: Longman;
    [Google Scholar]
  26. Stock J., Ninfa A. J., Stock A. M. 1989; Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiological Reviews 53:450–490
    [Google Scholar]
  27. Unden G., Trageser M. 1991; Oxygen regulated gene expression in Escherichia coli: control of anaerobic respiration by the FNR protein. Antonie van Leeuwenhoek 59:65–76
    [Google Scholar]
  28. Wood D., Darlison M. G., Wilde R. J., Guest J. R. 1984; Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Biochemical Journal 222:519–534
    [Google Scholar]
  29. Wooos D. D. 1953; The integration of research on the nutrition and metabolism of micro-organisms. Journal of General Microbiology 9:151–173
    [Google Scholar]
  30. Woods S. A., Guest J. R. 1987; Differential roles of the Escherichia coli fumarases and fnr-dependent expression of fumarase Band aspartase. FEMS Microbiology Letters 48:219–224
    [Google Scholar]
  31. Woods S. A., Schwartzbach S. D., Guest J. R. 1988; Two biochemically-distinct classes of fumarase in Escherichia coli. Biochimica et Biophysica Acta 954:14–26
    [Google Scholar]
  32. Zhang X., Ebright R. H. 1990; Substitution of 2 base pairs (1 base pair per DNA half-site) within the Escherichia coli lac promoter DNA site for catabolite gene activator protein places the lac promoter in the FNR regulon. Journal of Biological Chemistry 265:12400–12403
    [Google Scholar]
  33. Zheng L., Andrews P. C., Hermodson M. A., Dixon J. E., Zalkin H. 1990; Cloning and structural characterization of porcine heart aconitase. Journal of Biological Chemistry 265:2814–2821
    [Google Scholar]
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