Hostname: page-component-8448b6f56d-cfpbc Total loading time: 0 Render date: 2024-04-23T20:28:12.364Z Has data issue: false hasContentIssue false

The mutagenicity of amino acid analogues in Coprinus lagopus

Published online by Cambridge University Press:  14 April 2009

Philippa J. Talmud
Affiliation:
Department of Botany and Microbiology, University College London
D. Lewis
Affiliation:
Department of Botany and Microbiology, University College London
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The amino acid analogues p-fluorophenylalanine (PFP) and ethionine (ETH) are strongly mutagenic in Coprinus lagopus. The most pronounced effect was found with suppressor mutations of the met-1 locus. PFP, at a concentration of 2·4 × 10−4 M, increased the mutation frequency 500 fold and ETH, at a concentration of 2·4 × 10−3 M, 30 fold over the spontaneous mutation frequency. From the spectrum of suppressors of the met-1 locus and the dominant revertants of the ad-82 locus, induced by analogue treatments, it was concluded that both analogues induce single base-change mutations. The dose response curves follow a sigmoid plot, revealing that within a certain range of analogue concentrations, muta-genesis is strongly dose dependent.

Using analogue resistant mutants, it has been shown that PFP mutagenesis is a function of its incorporation into protein. However, ETH mutagenesis is independent of protein incorporation but can be correlated with the degree of ethylation of nucleic acids. The synergistic effect PFP and ETH supports the evidence of the different mutagenic actions of the two analogues.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1974

References

REFERENCES

Arnstein, H. R. V. & Richmond, M. H. (1964). The utilization of p-fluorophenylalanine for protein synthesis by the phenylalanine incorporation system from rabbit reticulocytes. Biochemical Journal 91, 340.CrossRefGoogle ScholarPubMed
Auerbach, C. (1969). Analysis of a case of mutagen specificity in Neurospora crassa. Ciba Foundation Symposium, ‘Mutation as cellular process’, p. 66.CrossRefGoogle Scholar
Auerbach, C. & Ramsay, D. P. (1967). Differential effect of incubation temperature on nitrous acid-induced reversion frequencies at two loci in Neurospora. Mutation Research 4, 508.CrossRefGoogle ScholarPubMed
Auerbach, C. & Ramsay, D. P. (1968). Analysis of a case of mutagen specificity in Neurospora crassa. 1. Dose response curves. Molecular and General Genetics 103, 72.CrossRefGoogle ScholarPubMed
Baker, R. & Tessman, I. (1968). Different mutagenic specificities in phages S13 and T4: in vivo treatment with N-methyl-N′-nitro-N-nitrosoguanidine. Journal of Molecular Biology 35, 439.CrossRefGoogle Scholar
Barker, C. E. (1970). Biochemical characterizations of mutants resistant para-fiuorophenyl-alanine in Coprinus lagopus. Ph.D. Thesis, University of London.Google Scholar
Böhme, H. (1967). Genetic instability of an ultraviolet sensitive mutant of Proteus mirabilis. Biochemical and Biophysical Research Communications 28, 191.CrossRefGoogle ScholarPubMed
Casselton, L. A. (1965). The production and behaviour of diploids in Coprinus lagopus. Genetical Research 6, 190.CrossRefGoogle ScholarPubMed
Drake, J. W. (1970). The Molecular basis of mutation. Holden-Day, San Francisco.Google Scholar
Faber, E. (1963). Ethionine carcinogenesis. Cancer Research 7, 383.CrossRefGoogle Scholar
Fowden, L., Lewis, D. & Tristram, H. (1967). Toxic amino acids: Their action as anti-metabolites. Advances in Enzymology 29, 89.Google Scholar
Friedman, M., Shull, K. & Faber, E. (1969). Highly selective in vivo ethylation of rat liver nuclear proteins by ethionine. Biochemical Biophysical Research Communications 34, 857.CrossRefGoogle Scholar
Grigg, G. W. (1952). Back mutation assay method in micro-organisms. Nature 169, 98.CrossRefGoogle ScholarPubMed
Janacek, J. (1967). Synthesis of β-galactosidase in Escherichia coli in the presence of phenylalanine analogues. Folia microbiologica (Praha) 12, 132.CrossRefGoogle Scholar
Janacek, J. & Rickenberg, H. V. (1964). The incorporation of β-2-thienylalanine into the β-galactosidase of Escherichia coli. Biochemica et Biophysica Acta 81, 108.Google Scholar
Janacek, J. & Spizek, J. (1969). The synthesis of β-galactosidase in Escherichia coli in the presence of 7-azatryptophan. Folia microbiologica (Praha) 14, 529.CrossRefGoogle Scholar
Jansen, G. J. O. (1972). Mutator activity in uvs mutants of Aspergillus nidulans. Molecular and General Genetics 116, 47.CrossRefGoogle ScholarPubMed
Kilbey, B. J. (1969). Allele-specific responses to factors that modify U.V. mutagenesis. Ciba Foundation Symposium, ‘Mutation as cellular process’, p. 50.CrossRefGoogle Scholar
Kølmark, H. G. (1956). Mutagenic properties of certain esters of inorganic acids investigated by the Neurospora back-mutation test. Comptes rendus des travaux du Laboratoire Carlsberg, Serie Physiologique 26, 206.Google Scholar
Langridge, J. (1968). Genetic and enzymatic experiments relating to the tertiary structure of β-galactosidase. Journal of Bacteriology 96, 1711.CrossRefGoogle Scholar
Lewis, C. M. & Tarrant, G. M. (1971). Induction of mutation by 5-fluorouracil and amino acid analogues in Ustilago maydis. Mutation Research 12, 349.CrossRefGoogle Scholar
Lewis, D. (1961). Genetical analysis of methionine suppressors in Coprinus. Genetical Research 2, 141.CrossRefGoogle Scholar
Lewis, D. (1963). Structural gene for the methionine activating enzyme and its mutation as a cause of resistance to ethionine. Nature 200, 151.CrossRefGoogle Scholar
Luria, S. E. & Delbrück, M. (1943). Mutations of bacteria from virus sensitivity to virus resistance. Genetics 28, 491.CrossRefGoogle ScholarPubMed
McBride, A. C. & Gowan, C. S. (1969). The induction of gene mutation and chromosome aberrations in Chlamydomonas eugametos by a phenylalanine analog. Genetical Research 14, 121.CrossRefGoogle ScholarPubMed
Mendonça, L. C. S. & Travassos, L. R. (1972). Metabolism of ethionine in ethionine-sensitive and ethionine-resistant cells of the enteric yeast Candida slooffi. Journal of Bacteriology 110, 643.CrossRefGoogle Scholar
Peterkovsky, A. (1965). In Transmethylation and methionine biosynthesis (eds. Shapiro, S. K. & Shlenk, F.) University of Chicago Press, Chicago, p. 137.Google Scholar
Rosen, L. (1968). Ethylation in vivo of purines in rat liver tRNA by L-ethionine. Biochemical Biophysical Research Communications 33, 546.CrossRefGoogle ScholarPubMed
Ruddick, J. & Runner, M. N. (1972). Ethionine as a depressant of synthesis and a source of label for DNA in chick embryos. Tetrology 5, 353.Google Scholar
Shahriari, H. & Casselton, L. A. (1973). By-pass and translational suppressors of methionine mutant in the fungus Coprinus lagopus. Abstract from the 171st meeting of the Genetical Society of Great Britain.Google Scholar
Shankel, D. M. (1962). ‘Mutation synergism’ of ultraviolet light and caffeine in Escherichia coli. Journal of Bacteriology 84, 410.CrossRefGoogle ScholarPubMed
Smith, J. D., Barnett, L., Brenner, S. & Russell, R. L. (1970). More mutant tyrosine transfer ribonucleic acids. Journal of Molecular Biology 54, 1.CrossRefGoogle ScholarPubMed
Speyer, J. F. (1965). Mutagenic DNA polymerase. Biochemical and Biophysical Research Communications 21, 6.CrossRefGoogle ScholarPubMed
Spizek, J. & Janacek, J. (1967). Effect of ethionine on the synthesis of β-galactosidase in Escherichia coli. Folia microbiologica (Praha) 14, 521.CrossRefGoogle Scholar
Spizek, J. & Janacek, J. (1969). Further observations on the effect of ethionine on the synthesis of β-galactosidase in Escherichia coli. Formation of an immunological cross-reacting protein. Folia microbiologica (Praha) 14, 521.CrossRefGoogle ScholarPubMed
Springgate, C. F. & Loeb, L. A. (1973). Mutagenic DNA polymerase in human leukaemic cells. Proceedings of the National Academy of Sciences of the U.S.A. 70, 245.CrossRefGoogle Scholar
Todd, N. K. & Casselton, L. A. (1972). Non-complementation between recessive suppressor gene mutations in Coprinus lagopus. Heredity 28, 274.Google Scholar
Tristram, H. & Neale, S. (1968). The activity and specificity of the proline permease in wild-type and analogue-resistant strains of Escherichia coli. Journal of General Microbiology 50, 211.CrossRefGoogle ScholarPubMed
Witkin, E. M. (1958). Post-irradiation metabolism and the timing of UV induced mutation in bacteria. Proceedings of the 10th International Congress of Genetics,Montreal1, 280.Google Scholar
Zimmermann, F. K., Schwaier, R. & von Laer, U. (1966). The effect of temperature on the mutation fixation in yeast. Mutation Research 3, 90.CrossRefGoogle ScholarPubMed