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Mechanism of suppression in Drosophila melanogaster* VIII. Comparison of su(s) alleles for ability to suppress the mutants purple, vermilion, and speck

Published online by Cambridge University Press:  14 April 2009

K. Bruce Jacobson ,
E. H. Grell ,
John J. Yim  and
April L. Gardner
K. Bruce Jacobson
Affiliation:
Biology Division, Oak Ridge National Laboratory, and University of Tennessee–Oak Ridge Graduate School of Biomedical Sciences, Oak Ridge, Tennessee 37830
E. H. Grell
Affiliation:
Biology Division, Oak Ridge National Laboratory, and University of Tennessee–Oak Ridge Graduate School of Biomedical Sciences, Oak Ridge, Tennessee 37830
John J. Yim
Affiliation:
Biology Division, Oak Ridge National Laboratory, and University of Tennessee–Oak Ridge Graduate School of Biomedical Sciences, Oak Ridge, Tennessee 37830
April L. Gardner
Affiliation:
Biology Division, Oak Ridge National Laboratory, and University of Tennessee–Oak Ridge Graduate School of Biomedical Sciences, Oak Ridge, Tennessee 37830
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The suppressor of sable [su(s)2] restores the function of vermilion (v), purple (pr) and speck (sp) as well as sable (s) in Drosophila melanogaster. In this report various alleles of su(s) are compared for their relative effectiveness on three target mutations, v, pr and sp. Three criteria for suppression of pr and v were employed: visible phenotype, eye pigment levels (drosopterins and xanthommatin) and enzyme levels (sepiapterin synthase and tryptophan oxygenase). For sp only the visible phenotype was examined. By all three criteria pr was found to be more easily suppressed than v; v and sp were comparable. By use of pr with various alleles of su(s) either homozygously or in heterozygous combination with su(s)+, the extent of suppression of pr can be best demonstrated by observing the levels of sepiapterin synthase; normal levels of drosopterins were found in females when sepiapterin synthase was only 20% of normal. On the other hand, the extent of suppression of v is best demonstrated by the amount of xanthommatin eye pigment, because even the suppressed vermilion fly has < 10% of wild-type activity of tryptophan oxygenase when 1-day-old flies are examined; in older flies this enzyme can be as high as 50% of wild type. From these results we also demonstrated that su(s)2, and other alleles, are not recessive but, in heterozygous combination with su(s)+, cause marked suppression of pr and slight, but reproducible, suppression of v. The purple mutation, therefore, is particularly useful for studying the mechanism of suppression as well as for obtaining new mutant alleles of su(s).

Type
Research Article
Information
Genetics Research , Volume 40 , Issue 1 , August 1982 , pp. 19 - 32
Copyright
Copyright © Cambridge University Press 1982

References

REFERENCES

Baglioni, C. (1960). Genetic control of tryptophan pyrrolase in Drosophila melanogaster and D. virilis. Heredity 15, 87–93.Google Scholar
Baillie, D. L. & Chovnick, A. (1971). Studies on the genetic control of tryptophan pyrrolase in Drosophila melanogaster. Molecular General Genetics 112, 341–383.CrossRefGoogle ScholarPubMed
Beadle, G. W. & Ephrussi, B. (1936). The differentiation of eye pigments in Drosophila as studied by transplantation. Genetics 21, 225–247.CrossRefGoogle ScholarPubMed
Beadle, G. W., Tatum, E. L. & Cloney, C. W. (1939). Development of eye colors in Drosophila: Production of v + hormone by fat bodies. Biological Bulletin 77, 407–414.Google Scholar
Bonnier, G. (1925). Note on the so-called vermilion duplication. Hereditas 7, 229–232.CrossRefGoogle Scholar
Butenandt, A., Biekert, E., Kubler, H. & Linzen, B. (1960). Uber Ommochrome XX. Zur Verbreitung der Ommatine in Tierreich Neue Methoden zu ihrer Identifizierung und quantitativen Bestimmung. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 319, 238–256.CrossRefGoogle Scholar
Casciano, D. A. & Gaertner, F. H. (1973). A specific and sensitive fluorometric assay for tryptophan oxygenase. Archives of Biochemistry Biophysics 156, 658–664.Google Scholar
Jacobson, K. B. (1971). Role of an isoacceptor transfer RNA as an enzyme inhibitor: Effect on tryptophan pyrrolase of Drosophila. Nature New Biology 231, 17–19.Google Scholar
Jacobson, K. B. (1978 a). A new substrate for formylkynurenine formamidase: N 1, N α- diformylkynurenine. Archives of Biochemistry and Biophysics 186, 84–88.Google Scholar
Jacobson, K. B. (1978 b). Mechanism of suppression in Drosophila. VII. Correlation between disappearance of an isoacceptor of tyrosine tRNA and the activation of the vermilion locus. Nucleic Acids Research 5, 2391–2404.Google Scholar
Jacobson, K. B., Calvino, J. F., Murphy, J. B. & Warner, C. K. (1975). Mechanism of suppression in Drosophila. II. Enzymatic discrimination of wild-type and suppressor tyrosine tRNA. Journal of Molecular Biology 93, 89–97.Google Scholar
Kikkawa, H. (1941). Mechanism of pigment formation in Bombyx and Drosophila. Genetics 26, 587–607.Google Scholar
Krivi, G. G. & Brown, G. M. (1979). Purification and properties of the enzymes from Drosophila melanogaster that catalize the synthesis of sepiapterin from dihydroneopterin triphosphate. Biochemical Genetics 17, 371–390.Google Scholar
Lindsley, D. L. & Grell, E. H. (1967). Genetic variation of Drosophila melanogaster. Carnegie Institute of Washington Publication, no. 627.Google Scholar
Lowry, O. H., Rosebraugh, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
Marzluf, G. A. (1965). Enzymatic studies with the suppressor of vermilion of Drosophila melanogaster. Genetics 52, 503–512.Google Scholar
Mischke, D., Kloetzel, P. & Schwochau, M. (1975). Tryptophan pyrrolase activity regulation in Drosophila: Role of an isoacceptor tRNA unsettled. Nature 255, 79–81.CrossRefGoogle ScholarPubMed
Pomato, N. (1974). The purification and characterization of tryptophan pyrrolase from Drosophila melanogaster. Ph.D. Thesis, University of Notre Dame.Google Scholar
Schultz, J. & Bridges, C. B. (1932). Methods for distinguishing between duplications and specific suppressors. American Naturalist 66, 323–324.CrossRefGoogle Scholar
Shapard, P. B. (1960). A physiological study of the vermilion eye color mutants of Drosophila melanogaster. Genetics 45, 359–376.Google Scholar
Sullivan, D. T. & Kitos, R. J. (1976). Developmental regulation of tryptophan catabolism in Drosophila. Insect Biochemistry 6, 649–655.Google Scholar
Tartof, K. D. (1969). Interacting gene systems. I. The regulation of tryptophan pyrrolase by the vermilion-suppressor of vermilion system in Drosophila. Genetics 62, 781–795.CrossRefGoogle ScholarPubMed
Tobler, J. E. (1975). Dosage compensation and ontogenic expression of suppressed and transformed vermilion flies in Drosophila. Biochemical Genetics 13, 29–43.CrossRefGoogle ScholarPubMed
Tobler, J. E., Yim, J. J., Grell, E. H. & Jacobson, K. B. (1979). Developmental changes of sepiapterin synthase activity associated with a variegated purple gene in Drosophila melanogaster. Biochemical Genetics 17, 197–206.Google Scholar
Wilson, T. G. & Jacobson, K. B. (1977). Isolation and characterization of pteridines from heads of D. melanogaster by a modified thin-layer chromatography procedure. Biochemical Genetics 15, 307–319.Google Scholar
Yim, J. J., Grell, E. H. & Jacobson, K. B. (1977). Mechanism of suppression in Drosophila: Control of sepiapterin synthase at the purple locus. Science 198, 1168–1170.Google Scholar