1887

Abstract

Summary: Glutamine synthetase (GS) (EC 6.3.1.2) was purified from an deletion strain containing the GS structural gene. The apparent of the cloned GS subunit was approximately 60000. This indicates a particle for the undissociated enzyme of 720000, assuming the enzyme is the typical dodecamer. Electron microscopy of purified GS revealed characteristic disc shaped molecules with central holes. The cloned GS was regulatedby Mg or Mn,adenylylation, and nitrogen source but was not affected by feedback modifiers. The GS has a -glutamyltransferase isoactivity point of pH 7.71.

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1986-07-01
2021-05-18
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References

  1. Barros M. E. C., Rawlings D. E., Woods D. R. 1985; Cloning and expression of the Thiobacillus ferrooxidans glutamine synthetase gene in Escherichia coli . Journal of Bacteriology 164:1386–1389
    [Google Scholar]
  2. Bender R. A., Janssen K. A., Resnick A. D., Blumenberg M., Foor F., Magasanik B. 1977; Biochemical parameters of glutamine synthetase from Klebsiella aerogenes . Journal of Bacteriology 129:1001–1009
    [Google Scholar]
  3. Bhandari B., Vairinhos F., Nicholas D. J. D. 1983; Some properties of glutamine synthetase from Rhizobium japonicum CC705 and CC723. Archives of Microbiology 136:84–88
    [Google Scholar]
  4. Bodasing S. J., Brandt P. W., Robb F. T., Woods D. R. 1985; Purification and regulation of glutamine synthetase in a collagenolytic Vibrio algino-lyticus strain. Archives of Microbiology 140:369–374
    [Google Scholar]
  5. Brown C. M. 1980; Ammonia assimilation and utilization in bacteria and fungi. In Microorganisms and Nitrogen Sources pp 511–535 Edited by Payne J. W. New York: John Wiley & Sons;
    [Google Scholar]
  6. Deuel T. F., Ginsburg A., Yeh J., Shelton E., Stadtman E. R. 1970; Bacillus subtilis glutamine synthetase. Journal of Biological Chemistry 245:5195–5205
    [Google Scholar]
  7. Frey T. G., Eisenberg D., Eiserling F. A. 1975; Glutamine synthetase forms three- and seven-stranded helical cables. Proceedings of the National Academy of Sciences of the United States of America 72:3402–3406
    [Google Scholar]
  8. Kaulen H., Klemme J. H. 1983; No evidence of covalent modification of glutamine synthetase in the thermophilic phototrophic bacterium Chloroflexus aurantiacus . FEMS Microbiology Letters 20:75–79
    [Google Scholar]
  9. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4 . Nature, London 227:680–685
    [Google Scholar]
  10. Lei M., Aebi U., Heidner E. G., Eisenberg D. 1979; Limited proteolysis of glutamine synthetase is inhibited by glutamate and by feedback inhibitors. Journal of Biological Chemistry 254:3129–3134
    [Google Scholar]
  11. O’Farrell P. H. 1975; High resolution two-dimensionai eieciropnoresis oi proteins. journal oj Biological Chemistry 250:4007–4021
    [Google Scholar]
  12. Ruvkun G. B., Ausubel F. 1980; Interspecies homology of nitrogenase genes. Proceedings of the National Academy of Sciences of the United States of America 77:191–195
    [Google Scholar]
  13. Shapiro B. M., Stadtman E. R. 1970; Glutamine synthetase (E. coli) . Methods in Enzymology 17A:910–922
    [Google Scholar]
  14. Shapiro B. M., Kingdon H. S., Stadtman E. R. 1967; Regulation of glutamine synthetase: a new form of the enzyme with altered regulatory and kinetic properties. Proceedings of the National Academy of Sciences of the United States of America 58:642–649
    [Google Scholar]
  15. Stadtman E. R., Ginsburg A. 1974; The glutamine synthetase of Escherichia coli: structure and control. In The Enzymes 3rd edn vol 10 pp 755–807 Edited by Boyer P. D. New York London: Academic Press;
    [Google Scholar]
  16. Streicher S. L., Tyler B. 1980; Purification of glutamine synthetase from a variety of bacteria. Journal of Bacteriology 142:69–78
    [Google Scholar]
  17. Towbin H., Staehelin T., Gordon J. 1979; Electrophoretic transfer of proteins from polyacrylamide gel to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences of the United States of America 76:4350–4354
    [Google Scholar]
  18. Tronick S. R., Ciardi J. E., Stadtman E. R. 1973; Comparative biochemical and immunological studies of bacterial glutamine synthetases. Journal of Bacteriology 115:858–868
    [Google Scholar]
  19. Tuovinen O. H., Kelly D. P. 1973; Studies on the growth of Thiobacillus ferrooxidans. I. Use of membrane filters and ferrous iron agar to determine viable numbers and comparison with 14CO2-fixation and iron oxidation as measures of growth. Archives of Microbiology 88:285–298
    [Google Scholar]
  20. Tuovinen O. H., Panda T. A., Tsuchiya H. M. 1979; Nitrogen requirements of iron-oxidising Thiobacillus for acidic ferric sulphate regeneration. Applied and Environmental Microbiology 37:954–958
    [Google Scholar]
  21. Tyler B. 1978; Regulation of the assimilation of nitrogen compounds. Annual Review of Biochemistry 47:1127–1162
    [Google Scholar]
  22. Wedler F. C., Hoffmann F. M. 1974; Glutamine synthetase of Bacillus stearothermophilus. I. Purification and basic properties. Biochemistry 13:3207–3214
    [Google Scholar]
  23. Wedler F. C., Shreve D. S., Kenney R. M., Ashour A. E., Carfi J., Rhee S. G. 1980; Two glutamine synthetases from Bacillus caldolyticus, an extreme thermophile. Journal of Biological Chemistry 255:9507–9516
    [Google Scholar]
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