1887

Abstract

SUMMARY: Mechanisms whereby and grow on L-histidinol as sole source of carbon and nitrogen have been examined.

Polyacrylamide gel electrophoresis (PAGE) showed two distinct histidinol dehydrogenase (HDH) bands in partially purified extracts: HDH(B) was always present but increased up to twofold by growth with histidine; HDH(I), additionally present only in histidinol-grown organisms, which had up to 10 times the total and specific HDH activity of organisms grown on salts+glucose medium. HDH biosynthesis was not repressed by histidine, glucose+ammonia or glutamate. HDH(I) could have evolved from HDH(B) by gene duplication and modification, with the resulting gene acquiring a new, inducible control mechanism.

A mutant, , of grew on histidinol as sole source of carbon and nitrogen, which the wild-type did only poorly. Only one HDH band was found on PAGE of partially purified extracts of either mutant or wild-type, however grown, though histidinol-grown showed a more intense band and 60 times the HDH activity of glucose+salts-grown organisms. Histidine, glucose+ammonia or glutamate abolished this HDH increase. Here the adaptation seemed to consist of an additional control mechanism giving rise to high levels of the normal HDH when histidinol was sole source of carbon and nitrogen.

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/content/journal/micro/10.1099/00221287-73-2-353
1972-11-01
2022-01-29
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References

  1. Adams E. 1954; The enzymatic synthesis of histidine from histidinol. Journal of Biological Chemistry 209:829–846
    [Google Scholar]
  2. Clarke J. J. 1964; Simplified ‘disc’ (polyacrylamide gel) electrophoresis. Annals of the New York Academy of Sciences 121:428–436
    [Google Scholar]
  3. Creaser E. H., Bennett D. J., Drysdale R. B. 1967; The purification and properties of histidinol dehydrogenase from Neurospora crassa . Biochemical Journal 103:36–41
    [Google Scholar]
  4. Lessie T. C., Neidhardt C. C. 1967; Formation and operation of the histidine-degrading pathway in Pseudomonas aeruginosa . Journal of Bacteriology 93:1800–1810
    [Google Scholar]
  5. 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]
  6. Mee B. J., Lee B. T. O. 1967; An analysis of histidine requiring mutants in Pseudomonas aeruginosa . Genetics 55:709–722
    [Google Scholar]
  7. Monod J., Cohn M. 1952; La biosynthèse induit des enzymes. Advances in Enzymology 13:67–119
    [Google Scholar]
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