1887

Microbiology Society logo

Volume 108, Issue 2

Mutants with Increased Sensitivity to Canavanine in the Fungus Free

Abstract

Mutants of with increased sensitivity to canavanine were derived from wild-type, -3 (presumably defective in carbamoyl-phosphate synthase for pyrimidine synthesis), (blocked in steps prior to arginine formation) and (blocked in steps prior to glutamate semialdehyde formation) strains, and were classified into eight distinct groups by genetic mapping. Four canavanine-sensitive genes () were allelic or very tightly linked to known loci. The pairs of genes involved were and (arginine requirer), and (citrulline requirer), and (citrulline requirer) and and (ornithine requirer). Another () was mapped in linkage group III.

A relationship was shown between the level of intracellular arginine and the extent of canavanine sensitivity; strains contain less intracellular arginine than the less sensitive wild-type. In most cases, this was shown to result from mutations affecting the enzyme(s) involved in arginine metabolism. and were thought to be affected in arginine- and ornithine-synthesizing enzymes, respectively. and exhibited a requirement for citrulline when the two genes were combined and were suggested to be loci specifying the two polypeptide chains of carbamoyl-phosphate synthase for arginine synthesis. was the locus controlling ornithine carbamoyltransferase. The metabolic lesions of the other mutants (, and ) were unclear.

Of the eight mutants, six could suppress and/or mutations: was able to suppress ; and were effective in suppressing ; suppressed both and The mechanism of the and suppressions was explained on the basis of metabolic cross-feeding.

  • Received:
  • Accepted:
  • Published Online:
© Society for General Microbiology 1978
Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-108-2-247
1978-10-01
2024-04-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/108/2/mic-108-2-247.html?itemId=/content/journal/micro/10.1099/00221287-108-2-247&mimeType=html&fmt=ahah

References

  1. Albrecht A. M., Scher W. I., Vogel H. J. 1962; Determination of aliphatic aldehydes by spectrophotometry. Analytical Chemistry 34:398–400
     [Google Scholar]
  2. Bauerle R. 1963; The metabolism of canavanine in a threonine-less mutant of Neurospora crassa. Ph.D. thesis, Purdue University Indiana, U.S.A:
     [Google Scholar]
  3. Bauerle R. H., Garner H. R. 1964; The assimilation of arginine and lysine in canavanine resistant and sensitive strains of Neurospora crassa . Biochimica et biophysica acta 93:316–322
     [Google Scholar]
  4. Bechet J., Grenson M., Wiame J. M. 1970; Mutants affecting the repressibility of arginine biosynthetic enzymes in Saccharomyces cerevisiae . European Journal of Biochemistry 12:31–39
     [Google Scholar]
  5. Cabet D., Gans M., Hirsch M. L., Prevost G. 1965; Mode d’action de deux gènes suppresseurs de l’effect des gènes ur-l-a chez Coprinus radiatus . Comptes rendus hebdomadaire des séances de l’Académie des sciences 261:5191–5194
     [Google Scholar]
  6. Cooke F., Tan H., Good H. M. 1969; An introduction to the genetics of the fungus Coniochaeta velutina . Canadian Journal of Botany 47:1019–1026
     [Google Scholar]
  7. Davis R. H. 1962; Consequences of a suppressor gene effective with pyrimidine and proline mutants of Neurospora. Genetics 47:351–360
     [Google Scholar]
  8. Davis R. H. 1967; Channelling in Neurospora metabolism. Organizational Biosynthesis303–322 Vogel H. J., Lampen J. O., Bryson V. New York: Academic Press;
     [Google Scholar]
  9. Davis R. H. 1968; Utilization of exogenous and endogenous ornithine by Neurospora crassa . Journal of Bacteriology 96:389–395
     [Google Scholar]
  10. Davis R. H. 1972; Metabolite distribution in cells. Science 178:835–840
     [Google Scholar]
  11. Davis R.H., Woodward V. W. 1962; The relationship between gene suppression and aspartate transcarbamylase activity in pyr-3 mutants of Neurospora. Genetics 47:1075–1083
     [Google Scholar]
  12. Davis R. H., Lawless M. B., Port L. A. 1970; Arginaseless Neurospora: genetics, physiology and polyamine synthesis. Journal of Bacteriology 102:299–305
     [Google Scholar]
  13. Doermamn A. A. 1954; A bioassay for lysine by use of a mutant of Neurospora. Journal of Bacteriology 49:315
     [Google Scholar]
  14. Kalyankar G. D., Ikawa M., Snell E. E. 1958; The enzymatic cleavage of canavanine to homoserine and hydroxy-guanidine. Journal of Biological Chemistry 233:1175–1177
     [Google Scholar]
  15. Kihara H., Snell E. E. 1957; The enzymatic cleavage of canavanine to o-ureidohomoserine and ammonia. Journal of Biological Chemistry 226:485–495
     [Google Scholar]
  16. Knivett V. A. 1954; The effect of arsenate on bacterial citrulline breakdown. Biochemical Journal 56:606–610
     [Google Scholar]
  17. Lacroute F., Pierard A., Grenson M., Wiame J. M. 1965; The biosynthesis of carbamyl phosphate in Saccharomyces cerevisiae . Journal of General Microbiology 40:127–142
     [Google Scholar]
  18. Logan J. B. 1969; Biochemistry and genetics of canavanine resistance in Neurospora. Ph.D. thesis, California Institute of Technology Pasadena, U.S.A:
     [Google Scholar]
  19. 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]
  20. Maas W. K. 1961; Studies on repression of arginine biosynthesis in Escherichia coli . Cold Spring Harbor Symposia on Quantitative Biology 26:183–191
     [Google Scholar]
  21. Markert C. L. 1952; Radiation-induced nutritional and morphological mutants of Glomerella. Genetics 37:339–352
     [Google Scholar]
  22. Mitchell M. B., Mitchell H. K. 1952; Observation on the behaviour of suppression in Neurospora. Proceedings of the National Academy of Sciences of the United States of America 38205–214
     [Google Scholar]
  23. Moyed H. S. 1964; Biochemical mechanisms of drug resistance. Annual Review of Microbiology 18:347–366
     [Google Scholar]
  24. Paterson M. C. 1969; Mutation studies on Coniochaeta velutina. M.Sc. thesis, Queen’s University Ontario, Canada:
     [Google Scholar]
  25. Paterson M. C., Tan H., Cooke F. 1969; Mutation spectrum in the fungus Coniochaeta velutina . Canadian Journal of Genetics and Cytology 11:870–879
     [Google Scholar]
  26. Reissig J. L., Issaly A. S., de Issaly J. M. 1967; Arginine-pyrimidine pathways in microorganisms. National Cancer Institute Monograph 27:259–271
     [Google Scholar]
  27. Richmond M. H. 1965; The enzymatic basis of specific antibacterial action by structural analogues. Biological Reviews 40:93–128
     [Google Scholar]
  28. Schwartz J. H., Maas W. K. 1960; Analysis of the inhibition of growth produced by canavanine in Escherichia coli . Journal of Bacteriology 79:794–799
     [Google Scholar]
  29. Suyama Y., Munkres K. D., Woodward V. W. 1959; Genetic analysis of the pyr-3 locus of Neurospora crassa : the bearing of recombination and gene conversion upon interallelic linearity. Genetica 30:293–311
     [Google Scholar]
  30. Tan H. 1968; An introduction to the genetics of the fungus Coniochaeta velutina. M.Sc. thesis, Queen’s University Ontario, Canada:
     [Google Scholar]
  31. Tan H. 1971; Canavanine sensitive mutants in Coniochaeta velutina. Ph.D. thesis, Queen’s University Ontario, Canada:
     [Google Scholar]
  32. Tan H., Cooke F. 1969; Arginine mutants and canavanine sensitivity in Coniochaeta velutina . Canadian Journal of Genetics and Cytology 11:483
     [Google Scholar]
  33. Van Pilsum J. E., Berman D. A., Wolin E. A. 1957; Assay and some properties of kidney transaminase. Proceedings of the Society for Experimental Biology and Medicine 9596–100
     [Google Scholar]
  34. Vogel H. J. 1956; A convenient growth medium for Neurospora. Microbial Genetics Bulletin 13:42–43
     [Google Scholar]
  35. Weglenski P. 1967; The mechanism of action of proline suppressors in Aspergillus nidulans . Journal of General Microbiology 47:77–85
     [Google Scholar]
  36. Wieland C.R., McDougall K. J. 1969; Suppression of pyr-3 mutants by am mutants in Neurospora. Genetics 61:2S62–S63
     [Google Scholar]
  37. Woodward V. W., Davis R.H. 1963; Coordinate changes in complementation, suppression and enzyme phenotypes of a pyr-3 mutant of Neurospora crassa . Heredity 18:21–25
     [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-108-2-247
Loading
Mutants with Increased Sensitivity to Canavanine in the Fungus Coniochaeta velutina
Microbiology 108, 247 (1978); https://doi.org/10.1099/00221287-108-2-247
/content/journal/micro/10.1099/00221287-108-2-247
/content/journal/micro/10.1099/00221287-108-2-247
Loading

Data & Media loading...

Most cited Most Cited RSS feed

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