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Volume 79, Issue 1

Control of Nitrogenase Synthesis in Free

Abstract

SUMMARY: Sulphate-limited continuous cultures of showed a proportional repression of nitrogenase activity with increasing concentrations of ammonium ion in the influent medium. A fully repressed population had a 50 % greater bacterial density than a fully derepressed one. On derepression, synthesis of nitrogenase lagged for 90 min after exhaustion of NH from the medium but was complete within one doubling time. Casamino acids did not decrease the pre-fixation lag obtained under sulphate-limited conditions in the chemostat. Longer lags were obtained when NH was exhausted under N-limited conditions. Such lags were decreased by Casamino acids, yeast extract, or -aspartate. Aspartate-N completely repressed nitrogenase under sulphate- or carbon-limited conditions but not under nitrogen limitation. In the initial stages of repression of nitrogenase synthesis by NH , apparent production of active enzyme continued for a short time in the absence of protein synthesis ; nitrogenase was then diluted out as the organisms multiplied. Repression by NH was at the level of mRNA transcription according to studies with rifampicin and chloramphenicol. ‘Coding capacity’ for nitrogenase synthesis declined with a half-life of about 4.5 min following inhibition of RNA synthesis with rifampicin. NH did not influence the decay rate but stimulated translation of such nitrogenase-specifying mRNA as had been initiated.

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© Society for General Microbiology, 1973
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1973-11-01
2023-04-01
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References

  1. Baker K. 1968; Low cost continuous culture apparatus. Laboratory Practice 17:817–824
     [Google Scholar]
  2. Blundell M., Craig E., Kennell D. 1972; Decay rates of different mRNA in E. coli and models of decay. Nature New Biology 238:46–49
     [Google Scholar]
  3. Campbell N. E. R., Evans H. J. 1969; Use of Pankhurst tubes to assay acetylene reduction by facultative and anaerobic nitrogen-fixing bacteria. Canadian Journal of Microbiology 15:1342–1343
     [Google Scholar]
  4. Chaney A. L., Marbach E. P. 1962; Modified reagents for determination of urea and ammonia. Clinical Chemistry 8:130–132
     [Google Scholar]
  5. Coffman R. L., Norris T. E., Koch A. L. 1971; Chain elongation rate of messenger and polypeptides in slowly growing Escherichia coli. Journal of Molecular Biology 60:1–19
     [Google Scholar]
  6. Daesch G., Mortenson L. E. 1972; Effect of ammonia on the synthesis and function of the N2-fixing enzyme system in Clostridium pasteurianum. Journal of Bacteriology 110:103–109
     [Google Scholar]
  7. Dixon R. A., Postgate J. R. 1972; Genetic transfer of nitrogen fixation from Klebsiella pneumoniae to Escherichia coli. Nature., London 237:102–103
     [Google Scholar]
  8. Drozd J. W., Postgate J. R. 1970; Effects of oxygen on acetylene reduction, cytochrome content and respiratory activity of Azotobacter chroococcum. Journal of General Microbiology 63:63–73
     [Google Scholar]
  9. Drozd J. W., Tubb R. S., Postgate J. R. 1972; A chemostat study of the effect of fixed nitrogen sources on nitrogen fixation, membranes and free amino acids in Azotobacter chroococcum. Journal of General Microbiology 73:221–232
     [Google Scholar]
  10. Eady R. R., Smith B. E., Cook K. A., Postgate J. R. 1972; Nitrogenase of Klebsiella pneumoniae. Biochemical Journal 128:655–675
     [Google Scholar]
  11. Hardy R. W. F., Knight E. Jun 1967; ATP-dependent reduction of azide and hydrogen cyanide by nitrogen-fixing enzymes of Azotobacter vinelandii and Clostridium pasteurianum. Biochimica et biophysica acta 139:69–90
     [Google Scholar]
  12. Hartman K. A., Nolan J. C., Amaya J. 1971; The dependence of the rate of RNase A catalysed hydrolysis of ribosomes and mRNA on the concentration of magnesium and ammonium ions. Biochemical and Biophysical Research Communications 45:1307–1311
     [Google Scholar]
  13. Hill S., Drozd J. W., Postgate J. R. 1972; Environmental effects on the growth of nitrogen-fixing bacteria. Journal of Applied Chemistry and Biotechnology 22:541–558
     [Google Scholar]
  14. Jacquet M., Kepes A. 1969; The step sensitive to catabolite repression and its reversal by 3′–5′ cyclic AMP during induced synthesis of β-galactosidase in E. coli. Biochemical and Biophysical Research Communications 36:84–92
     [Google Scholar]
  15. Kepes A. 1969; Transcription and translation in the lactose operon of Escherichia coli studied by in vivo kinetics. In Progress in Biophysics and Molecular Biology 19 pp 199–236 Edited by Butler J. A. V., Noble D. Oxford and London: Pergamon Press;
     [Google Scholar]
  16. Klucas R. 1972; Nitrogen fixation by Klebsiella grown in the presence of oxygen. Canadian Journal of Microbiology 18:1845–1850
     [Google Scholar]
  17. Lindsay H. L. 1963 Physiological studies of nitrogen fixation by cells and cell-free extracts of Aerobacter aerogenes Ph.D. Thesis, University of Wisconsin; Madison, Wisconsin, U.S.A.:
     [Google Scholar]
  18. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
     [Google Scholar]
  19. Lubin M., Ennis H. L. 1964; On the role of intracellular potassium in protein synthesis. Biochimica et biophysica acta 80:614–631
     [Google Scholar]
  20. Mahl M. C., Wilson P. W. 1968; Nitrogen fixation by cell-free extracts of Klebsiella pneumoniae. Canadian Journal of Microbiology 14:33–38
     [Google Scholar]
  21. Mandelstam J. 1962; The repression of constitutive β-galactosidase in Escherichia coli by glucose and other carbon sources. Biochemical Journal 82:489–493
     [Google Scholar]
  22. Miskin R., Zamir A., Elson D. 1970; Inactivation and reactivation of ribosomal subunits: the peptidyl transferase activity of the 50s subunit of Escherichia coli. Journal of Molecular Biology 54:355–378
     [Google Scholar]
  23. Parejko R. A., Wilson P. W. 1970; Regulation of nitrogenase synthesis by Klebsiella pneumoniae. Canadian Journal of Microbiology 16:681–685
     [Google Scholar]
  24. Patil R. B., Pengra R. M., Yoch D. C. 1967; Effects of nitrogen supplements on nitrogen fixation by Aerobacter aerogenes. Biochimica et biophysica acta 136:1–5
     [Google Scholar]
  25. Pengra R. M., Wilson P. W. 1958; Physiology of nitrogen fixation by Aerobacter aerogenes. Journal of Bacteriology 75:21–25
     [Google Scholar]
  26. Postgate J. R. 1972; The acetylene reduction test for nitrogen fixation. In Methods in Microbiology 6B pp 343–556 Edited by Norris J. R., Ribbons D. W. London and New York: Academic Press;
     [Google Scholar]
  27. Rigano C., Violante U. 1973; Effect of nitrate, ammonia and nitrogen starvation on the regulation of nitrate reductase in Cyanidium caldarium. Archiv für Mikrobiologie 90:27–33
     [Google Scholar]
  28. St John R. T., Brill W. J. 1972; Inhibitory effect of methylalanine on glucose-grown Azotobacter vinelandii. Biochimica et biophysica acta 261:63–69
     [Google Scholar]
  29. Shah V. K., Davis L. C., Brill W. J. 1972; Nitrogenase. 1. Repression and derepression of the iron– molybdenum and iron proteins in Azotobacter vinelandii. Biochimica et biophysica acta 256:498–511
     [Google Scholar]
  30. Sippel A., Hartman G. 1968; Mode of action of rifamycin on the RNA polymerase reaction. Biochimica et biophysica acta 157:218–219
     [Google Scholar]
  31. Strandberg G. W., Wilson P. W. 1968; Formation of the nitrogen-fixing enzyme system in Azotobacter vinelandii. Canadian Journal of Microbiology 14:25–31
     [Google Scholar]
  32. Streicher S. L., Gurney E. G., Valentine R. C. 1972; The nitrogen fixation genes. Nature, London 239:495–499
     [Google Scholar]
  33. Wilson P. W., Hull J. F., Burris R. H. 1943; Competition between free and combined nitrogen in nutrition of Azotobacter. Proceedings of the National Academy of Sciences of the United States of America 29:289–294
     [Google Scholar]
  34. Yoch D. C., Pengra R. M. 1966; Effect of amino acids on the nitrogenase system of Klebsiella pneumoniae. Journal of Bacteriology 92:618–622
     [Google Scholar]
  35. Zumft W. G., Cretney W. G., Huang T. C., Mortenson L. E., Palmer G. 1972; On the structure and function of nitrogenase from Clostridium pasteurianum W5. Biochemical and Biophysical Research Communications 48:1525–1532
     [Google Scholar]
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Control of Nitrogenase Synthesis in Klebsiella pneumoniae
Microbiology 79, 103 (1973); https://doi.org/10.1099/00221287-79-1-103
/content/journal/micro/10.1099/00221287-79-1-103
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