1887

Abstract

Summary: Thirty-one tryptophan-requiring mutants of have been assigned by genetic and complementation analyses to four loci designated and The and loci were located in group III and in group G of the linkage map. The locus showed no linkage to the other loci or to markers in three additional linkage groups tested. From auxanographic tests and a study of accumulated biosynthetic intermediates, the enzymes controlled by each locus have been provisionally assigned. The and loci both appear necessary for anthranilate synthetase activity since mutants accumulated no intermediates. Only the mutant could utilize anthranilic acid, therefore the locus must also be involved in a subsequent step in the pathway. The mutants utilized indole and accumulated anthranilic acid, and hence this locus is involved in the conversion of anthranilic acid to indoleglycerol phosphate. The mutants utilized only tryptophan and accumulated indoleglycerol phosphate and anthranilic acid. They are therefore blocked in the final steps of the pathway catalysed by tryptophan synthetase.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-93-1-126
1976-03-01
2024-04-27
Loading full text...

Full text loading...

/deliver/fulltext/micro/93/1/mic-93-1-126.html?itemId=/content/journal/micro/10.1099/00221287-93-1-126&mimeType=html&fmt=ahah

References

  1. Ahmad M., Choudhury MD. K. U., Islam S. M. 1969; Complementation and recombination between indole utilising tryptophan-3 mutants of Neurospora crassa. Heredity 24:656–660
    [Google Scholar]
  2. Anderson G. E. 1971 The Life History and Genetics of Coprinus lagopus Weston-super-Mare, Somerset: Harris Biological Supplies Ltd;
    [Google Scholar]
  3. Arryo-Begovich A., DeMoss J. A. 1973; The isolation of the components of the anthranilate synthetase complex from Neurospora crassa. Journal of Biological Chemistry 248:1262–1267
    [Google Scholar]
  4. Bonner D. M., DeMoss J. A., Mills S. E. 1965; The evolution of an enzyme. In Evolving Genes and Proteins pp. 305–318 Bryson V., Vogel H. J. Edited by New York and London: Academic Press;
    [Google Scholar]
  5. Casselton L. A., Casselton P. J. 1966; Control of fruiting of Coprinus lagopus on certain synthetic media. Transactions of the British Mycological Sociey 49:579–581
    [Google Scholar]
  6. Crawford I. P. 1975; Gene rearrangements in the evolution of the tryptophan synthetic pathway. Bacteriological Reviews 39:87–120
    [Google Scholar]
  7. DeMoss J. A., Jackson R. W., Chalmers J. H. 1967; Genetic control of the structure and activity of an enzyme aggregate in the tryptophan pathway of Neurospora crassa. Genetics 56:413–424
    [Google Scholar]
  8. Doy C. H., Gibson F. 1959; I-(o-Carboxylphenylamino)-I-deoxyribulose. A compound formed by mutant strains of Aerobacter aerogenes and Escherichia coli blocked in the biosynthesis of tryptophan. Biochemical Journal 72:586–597
    [Google Scholar]
  9. Guerdoux J.-L. 1967; Induction de la cynur’ninase par la cynur’nine, les tryptophane et 5-m’thyl-tryptophane chez le Coprinus radiatus. Comptes rendus hebdomadiare des séances de I’Académie des sciences D 265:681–684
    [Google Scholar]
  10. Henke H., Guerdoux J.-L., Hutter R. 1973; Relations entre les gènes et les enzymes de la biosynthèse du tryptophane chez le Coprinus radiatus. Comptes rendus hebdomadaire des seances de I’Académie des sciences D 276:2001–2004
    [Google Scholar]
  11. Hutter R., DeMoss J. A. 1967; Organisation of the tryptophan pathway: a phylogenetic study of the fungi. Journal of Bacteriology 94:1896–1907
    [Google Scholar]
  12. Lewis D. 1961; Genetical analysis of methionine suppressors in Coprinus. Genetical Research 2:141–155
    [Google Scholar]
  13. Manney T. R., Duntze W., Janosko N., Salazar J. 1969; Genetic and biochemical studies of partially active tryptophan synthetase mutants of Saccharomyces cerevisiae. Journal of Bacteriology 99:590–596
    [Google Scholar]
  14. Matchett W. H., DeMoss J. A. 1963; Direct evidence for a tryptophan-anthranilic acid cycle in Neurospora. Biochimica et biophysica acta 71:632–642
    [Google Scholar]
  15. Moore D. 1967; Four new linkage groups in Coprinus lagopus. Genetical Research 9:331–342
    [Google Scholar]
  16. Moore D., Stewart G. R. 1971; Mutants of Coprinus lagopus selected for resistance to 2-deoxy-d-glucose. Genetical Research 18:341–352
    [Google Scholar]
  17. Roberts C. F. 1967; Complementation analysis of the tryptophan pathway in Aspergillus nidulans. Genetics 55:233–239
    [Google Scholar]
  18. Yanofsky C. 1955; Tryptophan synthetase from Neurospora. In Methods in Enzymology 2 pp. 233–238 Colowick S. P., Kaplan N. O. Edited by New York and London: Academic Press;
    [Google Scholar]
  19. Yanofsky C. 1956; The enzymatic conversion of anthranilic acid to indole. Journal of Biological Chemistry 223:171–184
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-93-1-126
Loading
/content/journal/micro/10.1099/00221287-93-1-126
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error