The Effect of Nitrogen Limitation on Catabolite Repression of Amidase, Histidase and Urocanase in Pseudomonas aeruginosa

References

1. Arst H.N. 1973; Nitrogen metabolite repression in Aspergillus nidulans.. Molecular and General Genetics 126:111–141
   [Google Scholar]
2. Brammar W.J., Clarke P.H. 1964; Induction and repression of Pseudomonas aeruginosa amidase. Journal of General Microbiology 37:307–319
   [Google Scholar]
3. Brammar W.J., Clarke P.H. 1967; Biochemical and genetic studies with regulator mutants of the Pseudomonas aeruginosa 8602 amidase system. Journal of General Microbiology 47:87–102
   [Google Scholar]
4. Brill W.J., Magasanik B. 1969; Genetic and metabolic control of histidase and urocanase in Salmonella typhimurium strain 15-59 . Journal of Biological Chemistry 244:5392–5402
   [Google Scholar]
5. De Crombrugghe B., Chen B., Anderson W., Nissley P., Gottesman M., Pastan I., Perlman R. 1971; Lac DNA, RNA polymerase and cyclic AMP receptor protein, cyclic AMP, lac repressor and inducer are the essential elements for controlled lac transcription. Nature New Biology 231:139–142
   [Google Scholar]
6. Hynes M.J. 1970; Induction and repression of amidase enzymes in Aspergillus nidulans. Journal of Bacteriology 103:482–487
   [Google Scholar]
7. Hynes M.J. 1972; Mutants with altered glucose repression of amidase enzymes in Aspergillus nidulans. Journal of Bacteriology 111:717–722
   [Google Scholar]
8. Hynes M.J. 1974; Effect of ammonium, l-glutamate and l-glutamine on nitrogen catabolism in Aspergillus nidulans. Journal of Bacteriology 120:1116–1123
   [Google Scholar]
9. Kelly M. 1961; An investigation of the action of Pseudomonas aeruginosa on amides and related compounds. Ph.D. Thesis University of London:
   [Google Scholar]
10. Kelly M., Clarke P.H. 1962; An inducible amidase produced by a strain of Pseudomonas aeruginosa. Journal of General Microbiology 27:305–316
    [Google Scholar]
11. Lessie T.G., Neidhardt F.C. 1967; Formation and operation of the histidine-degrading pathway in Pseudomonas aeruginosa. Journal of Bacteriology 93:1800–1810
    [Google Scholar]
12. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. 1951; Protein measurements with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
13. Magasanik B., Prival M.J., Brenchley J.E., Tyler B.M., Deleo A.B., Streicher S.L., Bender R.A., Paris C.G. 1974; Glutamine synthesis as a regulator of enzyme synthesis. Current Topics in Cellular Regulation 8:119–138
    [Google Scholar]
14. Potts J.R. 1975; Histidine catabolism in Pseudomonas aeruginosa. Ph.D. Thesis University of London;
    [Google Scholar]
15. Potts J.R., Clarke P.H. 1974; The regulation of histidine catabolism in Pseudomonas aeruginosa. Society for General Microbiology Proceedings 1:63
    [Google Scholar]
16. Prival M.J., Brenchley J.E., Magasanik B. 1973; Glutamine synthetase and the regulation of histidase formation in Klebsiella aerogenes. Journal of Biological Chemistry 248:4334–4344
    [Google Scholar]
17. Prival M.J., Magasanik B. 1971; Resistance to catabolite repression of histidase and proline oxidase during nitrogen-limited growth. Journal of Biological Chemistry 246:6288–6296
    [Google Scholar]
18. Smyth P. F. 1974; Catabolite repression in Pseudomonas aeruginosa. Ph.D. Thesis University of London:
    [Google Scholar]
19. Smyth P.F., Clarke P.H. 1975a; Catabolite repression of Pseudomonas aeruginosa amidase: The effect of carbon sources on amidase synthesis. Journal of General Microbiology 90:81–90
    [Google Scholar]
20. Smyth P.F., Clarke P.H. 1975b; Catabolite repression in Pseudomonas aeruginosa amidase: Isolation of promotor mutants. Journal of General Microbiology 90:91–99
    [Google Scholar]
21. 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]
22. Tyler B., Deleo A.B., Magasanik B. 1974; Activation of hut DNA by glutamine synthetase. Proceedings of the National Academy of Sciences of the United States of America 71:225–229
    [Google Scholar]