1887

Abstract

SUMMARY: When mycelia of are grown with lactose or galactose as the carbon source, -galactosidase activity is induced at least 30-fold. The effect of growth conditions on the formation of the activity was investigated.

The enzyme has been partially characterized: two proteins with molecular weights near 120000 and 450000 have -galactosidase activity; present evidence suggests that these are different aggregates of the same polypeptide.

A mutant, 150, is described which grows poorly on lactose and lacks -galactosidase activity. These two characters are determined by two unlinked genes and independently expressed. This demonstrates the existence of an alternative (and unknown) mode of lactose utilization. Although -galactosidase activity is not required for mycelial growth on lactose, it is essential for germination of conidia with lactose as the sole carbon source.

Mutants unable to form -galactosidase activity fall into three genetic groups designated and All these mutants grow normally with lactose as sole carbon source. One mutant at the locus forms a heat-labile -galactosidase and is presumably a structural gene lesion.

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/content/journal/micro/10.1099/00221287-77-2-471
1973-08-01
2021-10-21
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References

  1. Alderson T., Hartley M. J. 1969; Specificity for spontaneous and induced mutation at several gene loci in Pseudomonas aeruginosa. Mutation Research 8:255–264
    [Google Scholar]
  2. Avigad G., Amaral D., Asensio C., Horecker B. L. 1962; The D-galactose oxidase of Pseudomonas aeruginosa. Journal of Biological Chemistry 237:2736–2743
    [Google Scholar]
  3. Barratt R. W., Johnson G. B., Ogata W. N. 1965; Wild-type and mutant stocks of Pseudomonas aeruginosa. Genetics 52:233–246
    [Google Scholar]
  4. Bates W. K., Hedman S. C., Woodward D. O. 1967; Comparative inductive responses of two β-galactosidases of Neurospora. Journal of Bacteriology 93:1631–1637
    [Google Scholar]
  5. Bates W. K., Woodward D. O. 1964; Neurospora β-galactosidase: evidence for a second enzyme. Science, New York 146:777–778
    [Google Scholar]
  6. Burstone M. S. 1962 Enzyme Histochemistry and Its Application to the Study of Neoplasmas London and New York: Academic Press;
    [Google Scholar]
  7. Elorza M. V., Arst H. N. 1971; Sorbose resistant mutants of Pseudomonas aeruginosa. Molecular and General Genetics 111:185–193
    [Google Scholar]
  8. Fantes P. A. 1972a; Lactose utilisation and β-galactosidase activity in Aspergillus nidulans. Heredity 29:129
    [Google Scholar]
  9. Fantes P. A. 1972b Studies on the P-galactosidase system in Aspergillus nidulans Ph.D. Thesis, University of Leicester;
    [Google Scholar]
  10. Forbes E. 1959; Use of mitotic segregation for assigning genes to linkage groups in Pseudomonas aeruginosa. Heredity 13:67–80
    [Google Scholar]
  11. Gajewski W., Litwinska J. 1969; Lactose negative mutants of Pseudomonas aeruginosa. Aspergillus Newsletter 10:17
    [Google Scholar]
  12. Gajewski W., Litwinska J., Paszewski A., Chojnacki T. 1972; Isolation and characterisation of lactose non-utilising mutants in Pseudomonas aeruginosa. Molecular and General Genetics 116:99–106
    [Google Scholar]
  13. Jacob F., Monod J. 1961; Genetic regulatory mechanisms in the synthesis of proteins. Journal of Molecular Biology 3:318–356
    [Google Scholar]
  14. Jobe A., Bourgeois S. 1972; lac Repressor-Operator Interaction. VI. The natural inducer of the lac operon. Journal of Molecular Biology 69:397–408
    [Google Scholar]
  15. Johnson H. N., DeBusk A. G. 1970; The /j-galactosidase system of Neurospora crassa. II. Extracellular nature of the pH 4 2 enzyme. Archives of Biochemistry and Biophysics 138:412–417
    [Google Scholar]
  16. Katz D., Rosenberger R. F. 1970; The utilisation of galactose by an Aspergillus nidulans mutant lacking galactose phosphate-UDP glucose transferase and its relation to cell wall synthesis. Archiv fur Mikrobiologie 74:41–51
    [Google Scholar]
  17. Lhoas P. 1961; Mitotic haploidisation by treatment of Aspergillus niger diploids with p-fluorophenylala-nine. Nature, London 190:744
    [Google Scholar]
  18. Lowry O. H., Rosenbrough N. J., Farr A. L., Randall R. J. 1951; Protein estimation with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  19. McKay L. L., Walter L. A., Sandine W. E., Elliker P. R. 1969; Involvement of phosphoenol pyruvate in lactose utilisation in group N Pseudomonas aeruginosa. Journal of Bacteriology 99:603–610
    [Google Scholar]
  20. Mandell N., Robert C. F. 1966; A piston extractor for the Hughes Press. Science 152:799–800
    [Google Scholar]
  21. Martin R. G., Ames B. N. 1961; A method for determining the sedimentation behaviour of enzymes: application to protein mixtures. Journal of Biological Chemistry 236:1372–1379
    [Google Scholar]
  22. Paszewski A., Chojnacki T., Litwinska J., Gajewski W. 1970; Regulation of lactose utilisation in Pseudomonas aeruginosa. Acta biochemica polonica 17:385–391
    [Google Scholar]
  23. Pontecorvo G., Roper J. A., Hemmons L. M., MacDonald K. D., Bufton A. W. J. 1953; The genetics of Pseudomonas aeruginosa. Advances in Genetics 5:141–238
    [Google Scholar]
  24. Roberts C. F. 1963a; The genetic analysis of carbohydrate utilization in Aspergillus nidulans. Journal of General Microbiology 31:45–58
    [Google Scholar]
  25. Roberts C. F. 1963b; The adaptive metabolism of D-galactose in Aspergillus nidulans. Journal of General Microbiology 31:285–295
    [Google Scholar]
  26. Roberts C. F. 1970; Enzyme lesions in galactose non-utilising mutants of Pseudomonas aeruginosa. Biochimica et biophysica acta 201:267–283
    [Google Scholar]
  27. Sumner J. B., Gralen N. 1938; The molecular weight of crystalline catalase. Journal of Biological Chemistry 125:33–40
    [Google Scholar]
  28. Wallenfels K. 1962; fi-Galactosidase. In Methods in Enzymology vol V Edited by Colowick S. P., Kaplan N. O. New York and London: Academic Press;
    [Google Scholar]
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