Summary
Maroon-like homozygotes are completely deficient for xanthine dehydrogenase (XDH) and aldehyde oxidase (AO), however ma-l is not a structural locus for either enzyme. Quantitative immunoelectrophoresis of ma-l and wild type extracts suggests that the ma-l function must be post-translational. To determine whether the ma-l function involves some direct physical changes in XDH and/or AO the enyzmes were characterized with respect to temperature sensitivity and behavior in gel sieving electrophoresis. Since the XDH and AO from complementary ma-l heterozygotes is more thermolabile and different in shape from wild type XDH and AO, we conclude that ma-l is involved in a post-translational modification of these enzymes.
Similar content being viewed by others
References
Andres, R.Y.: Aldehyde oxidase and xanthine dehydrogenase from wild type Drosophila melanogaster and immunologically cross-reacting material from ma-l mutants. Eur. J. Biochem. 62, 591–600 (1976)
Baker, B.S.: The maternal and zygotic control of development by cinnamon, a new mutant in Drosophila melanogaster. Dev. Biol. 33, 429–440 (1973)
Bray, R.C.: Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In: The enzymes, Vol. XII, Part B (P. Boyer, ed.). San Francisco: Academic Press 1976
Bunn, F.H., Gabbay, K.H., Gallop, P.M.: The glycosylation of hemoglobin: relevance to diabetes mellitus. Science 200, 21–27 (1978)
Chovnick, A., Ballantyne, G.H., Baillie, D.L., Holm, D.G.: Gene conversion in higher organisms: half-tetrad analysis of recombination within the rosy cistron of Drosophila melanogaster. Genetics 66, 315–329 (1970)
Chovnick, A., Finnerty, V., Schalet, A., Duck, P.: Studies on genetic organization in higher organisms: I. Analysis of a complex gene in Drosophila melanogaster. Genetics 62, 145–160 (1969)
Chovnick, A., Gelbart, W., McCarron, M.: Organization of the rosy locus in Drosophila melanogaster. Cell 11, 1–10 (1977)
Chovnick, A., Gelbart, W., McCarron, M., Osmond, B., Candido, E.P.M., Baillie, D.L.: Organization of the rosy locus in Drosophila melanogaster: Evidence for a control element adjacent to the xanthine dehydrogenase structural element. Genetics 84, 233–255 (1976)
Chovnick, A., McCarron, M., Gelbart, W., Pandey, J.: Electrophoretic variants as a tool in the analysis of gene organization in higher organisms. In: Isozymes, Vol. IV. New York: Academic Press 1975
Chrambach, A., Rodbard, D.: Polyacrylamide gel electrophoresis. Science 172, 440–451 (1971)
Cochrane, B., Richmond, R.: Studies of esterase-6 in Drosophila melanogaster. I. The genetics of a post-translational modification. Biochem. Genet., in press (1979)
Dickinson, W.J.: The genetics of aldehyde oxidase in Drosophila melanogaster. Genetics 66, 487–496 (1970)
Dickinson, W.J., Sullivan, D.T.: Gene-enzyme systems in Drosophila. Berlin-Heidelberg-New York: Springer 1975
Dickinson, W.J., Weisbrod, E.: Gene regulation in Drosophila: Independent expression of closely linked, structural loci. Biochem. Genet. 14, 709–721 (1976)
Dizik, M., Elliot, R.W.: A gene apparently determining the extent of sialylation of lysosomal α-mannosidase in mouse liver. Biochem. Genet. 15, 31–46 (1977)
Dizik, M., Elliot, R.W.: A second gene affecting the sialylation of lysosomal α-mannosidase in mouse liver. Biochem. Genet. 16, in press (1978)
Finnerty, V.G., Duck, P., Chovnick, A.: Studies on genetic organization in higher organisms. II. Complementation and fine structure of the maroon-like locus of Drosophila melanogaster. Proc. Natl. Acad. Sci. U.S.A. 65, 939–946 (1970)
Finnerty, V.: The simple cistrons. In: The genetics and biology of Drosophila. Vol. I, pp. 721–760 (E. Novitski, M. Ashburner, eds.). New York: Academic Press 1976
Finnerty, V., Johnson, G.: Post-translational modification as a potential explanation of high levels of enzyme polymorphism. I. Modification of xanthine dehydrogenase and aldehyde oxidase in Drosophila melanogaster. Genetics, in press (1979)
Forrest, H.S., Hanly, E.W., Lagowski, J.M.: Biochemical differences between the mutants rosy-2 and maroon-like of Drosophila melanogaster. Genetics 46, 1455–1463 (1961)
Gelbart, W., McCarron, M., Chovnick, A.: Extension of the limits of the XDH structural elements. Genetics 84, 211–232 (1976)
Glassman, E., Pinkerton, W.: Complementation at the maroon-like eye-color locus of Drosophila melanogaster. Science 131, 1810–1811 (1960)
Greengard, P.: Phosphorylated proteins as physiological effectors. Science 189, 146–152 (1978)
Johnson, G.: Analysis of enzyme variation in natural populations of the butterfly Colias eurytheme. Proc. Natl. Acad. Sci. U.S.A. 68, 997–1001 (1971)
Johnson, G.: Characterization of electrophoretically cryptic variation in the alpine butterfly Colias meadii. Biochem. Genet 15, 665–693 (1977)
Joly, M.: A physico-chemical approach to the denaturation of proteins. Molecular biology series, Vol. 6. New York: Academic Press 1965
Karam, J.D.: Studies on the three loci which control xanthine dehydrogenase in Drosophila melanogaster. Ph. D. dissertation, Univ. of North Carolina. Chapel Hill, N.C., 1965
Keller, E.C., Glassman, E.: Phenocopies of the ma-l and ry mutants of Drosophila melanogaster: Inhibition in vivo of xanthine dehydrogenase by 4-hydroxypyrazolo (3,4-d) pyrimidine, Nature 208, 202–203 (1965)
Langridge, J.: Genetics and enzymatic experiments relating to the tertiary structure of β-galactosidase. J. Bacteriol. 96, 1711–1717 (1968)
Laurell, C.B.: Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal. Biochem. 15, 45–52 (1966)
Lehmann, H., Carrell, R.W.: Variations in the structure of human haemoglobin with particular reference to the unstable haemoglobins. Brit. Med. Bull. 25, 14–23 (1969)
Matheson, D.W., Bruce, R.L., Beauchamp, K.L.: The t tests. In: Introduction to experimental psychology, 2nd ed., pp. 323–333. Holt, Rinehart and Winston, Inc. U.S.A.
McCarron, M., Gelbart, W., Chovnick, A.: Intracistronic mapping of electrophoretic sites in Drosophila melanogaster: fidelity of information transfer by gene conversion. Genetics 76, 289–299 (1974)
Nason, A., Lee, K.Y., Pan, S., Erickson, R.: Evidence for a molybdenum cofactor common to all molybdenum enzymes based on the in vitro assembly of assimilatory NADPH-nitrate reductase using the Neurospora mutant nit-1. Proc. Climax 1st Int. Conf. on Chemistry and uses of molybdenum, U. of Reading, England. Held in Sept. 1973 (1974)
Uy, R., Wold, F.: Post-translational covalent modification of proteins. Science 198, 890–896 (1977)
Weeke, B.: Rocket immunoelectrophoresis. In: A manual of quantitative immunoelectrophoresis: methods and applications (N.H. Axelson, J. Kroll, B. Weeke, eds.). Scand. J. Immunol. 2 (Suppl. 1), 37–46 (1973)
Author information
Authors and Affiliations
Additional information
Communicated by M.M. Green
Rights and permissions
About this article
Cite this article
Finnerty, V., McCarron, M. & Johnson, G.B. Gene expression in Drosophila: Post-translational modification of aldehyde oxidase and xanthine dehydrogenase. Molec. Gen. Genet. 172, 37–43 (1979). https://doi.org/10.1007/BF00276213
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00276213