Hostname: page-component-586b7cd67f-t7czq Total loading time: 0 Render date: 2024-11-23T07:36:16.476Z Has data issue: false hasContentIssue false
  • English
  • Français

Studies on the inhibition and mutation of Aspergillus nidulans by acridines

Published online by Cambridge University Press:  14 April 2009

C. Ball  and
J. A. Roper
C. Ball
Affiliation:
Department of Genetics, University of Sheffield
J. A. Roper
Affiliation:
Department of Genetics, University of Sheffield
Rights & Permissions [Opens in a new window]

Extract

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.

A number of acridines have been tested for ability to inhibit conidia of strains of Aspergillus nidulans. The effectiveness of any one acridine in growth inhibition and killing involves interaction of genotype and conditions of treatment such as temperature, pH, treatment medium and light intensity. Mutant alleles which confer growth resistance to acriflavine are selective in their actions towards other acridines, may differ in their dominance relationships with different acridines and are even selective with regard to the conditions under which they confer acriflavine resistance. Certain pairs of acridines, used simultaneously, show additive effects, potentiation, or annulment by one of inhibition caused by the other.

Some of these findings have been applied in a study of factors affecting acridine-induced mutation in Aspergillus conidia. Under conditions which permit metabolism, acriflavine induces a high frequency of unstable morphological variants. One such variant has been shown to be a disomic. Using a system of reversion from auxotrophy to prototrophy, acriflavine-induced mutation has been obtained both with high light intensities and in the absence of light. In the latter case recombination as a feature of the mutation process is excluded.

Type
Research Article
Information
Genetics Research , Volume 7 , Issue 2 , April 1966 , pp. 207 - 221
Copyright
Copyright © Cambridge University Press 1966

References

REFERENCES

Albert, A. (1960). Selective toxicity. London: Methuen.Google Scholar
Brenner, S., Barnett, L., Crick, F. H. C. & Orgel, A. (1961). The theory of mutagenesis. J. molec. Biol. 3, 121–4.CrossRefGoogle Scholar
Brockman, H. E. Unpublished. Quoted by De Serres, F. J. (1964). J. cell. comp. Physiol. 64, (Suppl. 1), 33–44.Google Scholar
Clutterbuck, A. J. & Roper, J. A. (1965). A direct determination of nuclear distribution in Aspergillus nidulans. Genet. Res. (In press).Google Scholar
De Mars, R. I. (1953). Chemical mutagenesis in bacteriophage T2. Nature, Lond. 172, 964.CrossRefGoogle Scholar
Drake, J. W. (1964). Studies on the induction of mutations in bacteriophage T4 by ultraviolet irradiation and by proflavine. J. cell. comp. Physiol. 64 (Suppl. 1), 19–32.CrossRefGoogle Scholar
Dulbecco, R. (1964). Summary of 1964 biology research conference. J. cell. comp. Physiol. 64, (Suppl. 1), 181—6.CrossRefGoogle ScholarPubMed
Dutta, G. P. (1965). Demonstration of neutral polysaccharides with fluorescence microscopy using acridine orange. Nature, Lond. 205, 712.CrossRefGoogle ScholarPubMed
Eisenstark, A. & Rosner, J. L. (1964). Chemically induced reversions in the cysC region of Salmonella typhimurium. Genetics, 49, 343–55.CrossRefGoogle ScholarPubMed
Forbes, E. (1959). Use of mitotic segregation for assigning genes to linkage groups in Aspergillus nidulans. Heredity, 13, 67–80.CrossRefGoogle Scholar
Grigg, G. W. (1952). Back mutation assay method in microorganisms. Nature, Lond. 169, 98–100.CrossRefGoogle ScholarPubMed
Hass, E. (1944). The effect of atebrin and quinine on isolated respiratory enzymes. J. biol. Chem. 155, 321–31.CrossRefGoogle Scholar
Hellerman, L.Lindsay, A. & Bovarnick, M. R. (1946). Inhibition of d-amino acid oxidase by competition with F.A.D. by atabrine, quinine and certain other drugs. J. biol. Chem. 163, 553–70.CrossRefGoogle Scholar
Hirota, Y. & Iijima, T. (1957). Acriflavine as an effective agent for eliminating F-factor in Escherichia coli K-12. Nature, Lond. 180, 655–6.CrossRefGoogle ScholarPubMed
Käfer, E. (1961). The processes of spontaneous recombination in vegetative nuclei of Aspergillus nidulans. Genetics, 46, 1581–1609.CrossRefGoogle ScholarPubMed
Lerman, L. S. (1963). The structure of the DNA-acridine complex. Proc. Natn. Acad. Sci., U.S.A. 49, 94–102.CrossRefGoogle ScholarPubMed
Lerman, L. S. (1964). Acridine mutagnes and DNA structure. J. cell. comp. Physiol. 64, (Suppl. 1), 1–18.CrossRefGoogle Scholar
Lilly, L. Y. (1965). An investigation of the suitability of the suppressors of meth1 in Aspergillus nidulans for the study of induced and spontaneous mutation. Mutation Research, 2, 192–5.CrossRefGoogle Scholar
McIlwain, H. (1941). A nutritional investigation of the anti-bacterial action of acriflavine. Biochem. J. 35, 1311–19.CrossRefGoogle Scholar
Magni, G. E., von Borstel, R. C. & Sora, S. (1964). Mutagenic action during meiosis and antimutagenic action during mitosis by 5-aminoacridine in yeast. Mutation Research, 1, 227–30.CrossRefGoogle Scholar
Morpurgo, G. (1961). Somatic segregation induced by p-fluorophenylalanine. Aspergillus Newsletter, 2, 10.Google Scholar
Pontecorvo, G., Roper, J. A., Hemmons, L. M., MacDonald, K. D. & Button, A. W. J. (1953). The genetics of Aspergillus nidulans. Adv. Genet. 5, 141–238.CrossRefGoogle ScholarPubMed
Reissig, J. L. (1964). Are acridines mutagenic for Neurospora? Neurospora Newsletter, 6, 16.Google Scholar
Ritchie, D. A. (1964). Mutagenesis with light and proflavine in phage T4. Genet. Res. 5, 168–9.CrossRefGoogle Scholar
Robbins, E. & Marcus, D. (1963). Dynamics of acridine orange-cell interactions. J. cell. Biol. 18, 237–50.CrossRefGoogle Scholar
Roper, J. A. & Käfer, E. (1957). Acriflavine-resistant mutants of Aspergillus nidulans. J. gen. Microbiol. 16, 660–7.CrossRefGoogle ScholarPubMed
Sevag, M. G. & Gots, J. S. (1948 a). Enzymatic studies on the mechanism of the resistance of pneumococcus to drugs. II The inhibition of dehydrogenase activities by drugs; antagonistic effects of riboflavin to inhibitions. J. Bact. 56, 723–35.CrossRefGoogle ScholarPubMed
Sevag, M. G. & Gots, J. S. (1948 b). Enzymatic studies on the mechanism of the resistance of pneumococcus to drugs. III Experimental results indicating alteration in enzyme proteins associated with the development of resistance to drugs. J. Bact. 56, 737–48.CrossRefGoogle ScholarPubMed
Siddiqi, O. H. (1962). Mutagenic action of nitrous acid on Aspergillus nidulans. Genet. Res. 3, 303–14.CrossRefGoogle Scholar
Speck, J. F. & Evans, E. A. (1945). The biochemistry of the malarial parasite. III The effect of quinines and atebrin on glycolysis. J. biol. Chem. 159, 83–96.CrossRefGoogle Scholar
Stouthamer, A. H., De Haan, P. G. & Bulten, E. J. (1963). Kinetics of F-curing by acridine orange in relation to the number of F-particles in Escherichia coli. Genet. Res. 4, 305–17.CrossRefGoogle Scholar
Warr, J. R. & Roper, J. A. (1965). Resistance to various inhibitors in Aspergillus nidulans. J. gen. Microbiol. (In press).CrossRefGoogle ScholarPubMed
Werr, R. B. & Kubitschek, H. E. (1963). Mutagenic and antimutagenic effects of acridine orange in Escherichia coli. Biochem. biophys. Res. Commun. 13, 90–4.Google Scholar