Summary
The molybdenum hydroxylases are a ubiquitous class of enzymes which contain molybdenum in association with a low molecular weight cofactor. Genetic evidence suggests that the Drosophila loci, ma-1, cin and lxd are concerned with this cofactor because mutants for any one of these loci simultaneously interrupt activity for two molybdenum hydroxylases, XDH and A0. A third enzyme activity, P0, is also absent in each of the three mutants but evidence classifying P0 as a molybdoenzyme has been lacking. This study utilizes the known tungsten sensitivity of molybdoenzymes to demonstrate directly that pyridoxal oxidase is also a molybdoenzyme. The low molecular weight molybdenum cofactor is found to be severely reduced in extracts of the lxd and cin mutants but ma-1 mutants have high levels of cofactor. A partially purified preparation of XDH crossreacting material from ma-1 was also shown to contain the molybdenum cofactor. These results, considered with data from other workers are taken to indicate that the functions of all three of the loci examined could be concerned with some aspect of cofactor biosynthesis.
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References
Andres R (1976) Aldehyde oxidase and xanthine dehydrogenase from wild type Drosophila melanogaster and immunologically crossreacting material from ma-1 mutants. Eur J Biochem 62:591–600
Baker BS (1973) The maternal and zygotic control of development by cinnamon, a new Mutant in Drosophila melanogaster. Dev Biol 33:429–440
Bray RC (1976) Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In: Boyer P (ed) The enzymes, vol XII, part B. Academic Press, San Francisco
Chovnick A, Finnerty V, Schalet A, Duck P (1969) Studies on genetic organization in higher organisms: I. Analysis of a complex gene in Drosophila melanogaster. Genetics 62:145–169
Coughlan MP, Johnson JL, Rajagopalan KV (1980) Mechanisms of molybdoenzymes by cyanide. J Biol Chem 255:2694–2699
Dickinson WJ (1970) The genetics of aldehyde oxidase in Drosophila melanogaster. Genetics 66:487–496
Dickinson WJ, Weisbrod E (1976) Gene regulation in Drosophila: Independent expression of closely lined, structured loci. Biochem Gen 14:709–721
Finnerty V, McCarron M, Johnson GB (1979) Gene expression in Drosophila: Posttranslational modification of aldehyde oxidase and xanthine dehydrogenase. Mol Gen Genet 172:37–43
Finnerty V, Johnson G (1979) Post-translational modification as a potential explanation of high levels of enzyme polymorphism. Modification of xanthine dehydrogenase and aldehyde oxidase in Drosophila melanogaster. Genetics 91:695–722
Forrest HS, Hanly EW, Lagowski JM (1961) Biochemical differences between the mutants rosy 2 and marron-like of Drosophila melanogaster. Genetics 46:1455–1463
Glassman E, Mitchell HK (1959) Mutants of Drosophila melanogaster deficient in Xanthine Dehydrogenase. Genetics 44:153–162
Hanly EW (1964) A Quantitative Assay for the Oxidase Activity Associated with Xanthine Dehydrogenase. Dros Info Service 39:82
Johnson JL, Hainline BE, Rajagopalan KV (1980) Characterization of the molybdenum cofactor of sulfite oxidase, xanthine oxidase and nitrate reductase. J Biol Chem 255:1783–1786
Johnson JL, Rajagopalan KV (1974) Molecular basis of the biological function of molybdenum effect of tungsten on xanthine oxidase and sulfite oxidase in the rat. J Biol Chem 249:849–866
Ketchum PA, Sevilla CL (1973) In vitro formation of nitrate reductase using extracts of the nitrate reductase mutant if Neurospora crassa, nit-1 and Rhodospirillum rubrum. J Bacteriol 116:600–609
Lee KY, Erickson R, Pan SS, Jones G, May F, Nason A (1974) Effect of tungsten and vanadium on the in vitro assembly of assimilatory nitrate reductase utilizing Neurospora mutant nit-1. J Biol Chem 249:3953–3959
Lindsley DL, Grell EH (1968) Genetic variations of Drosophila melanogaster. Carnegie Institute of Washington Public No 627, Oak Ridge
Nason A, Antoine AD, Ketchum PA, Frazier WA, Lee DK (1970) Formation of assimilatory nitrate reductase by in vitro inter-cistronic complementation in Neurospora crassa. Proc Natl Acad Sci USA 65:137–144
Nason A, Lee KY, Pan S, Erickson RH (1974) 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 First Int Conf on Chemistry and Uses of Molybdenum, Univ of Reading, England, Sept 1973, Mitchell PCH (ed) Climax Molybdenum Company Limited, London
Nason A, Lee KY, Pan S, Ketchum PA, Lamberti A, DeVries J (1971) In vitro formation of assimilatory reduced nicotinamide adenine dinucleotide phosphate: Nitrate reductase from a Neurospora mutant and a component of molybdenum-enzymes. Proc Natl Acad Sci USA 68:3242–3246
O'Brien SJ, MacIntyre RJ (1978) Genetics and biochemistry of enzymes and specific proteins of Drosophila, chap 8. In: Ashburner M, Wright TRF (eds) The Genetics and Biology of Drosophila 2A. Academic Press, London
Pateman JA, Cove DJ, Rever BM, Roberts DB (1964) A common cofactor for nitrate reductase and xanthine dehydrogenase which also regulates the synthesis of nitrate reductase. Nature 201:58–60
Pienkos PT, Shah VK, Brill WJ (1977) Molybdenum cofactors from molybdoenzymes and in vitro reconstitution of nitrogenase and nitrate reductase. Proc Natl Acad Sci USA 74:5468–5471
Scazzocchio C (1980) The genetics of the molybdenum-containing enzymes, chap 16. In: Coughlan MP (ed) Molybdenum and molybdenum-containing enzymes. Pergamon Press, New York
Warner CK, Watts DT, Finnerty V (1980) Molybdenum hydroxylases in Drosophila 1. Preliminary studies of pyridoxal oxidase. Mol Gen Genet 180:449–453
Weeke B (1973) Rocket immunoelectrophoresis ch 2. A manual of quantitative immunoelectrophoresis. Methods and applications. Axelsen NH, Kroll J, Weeke B (eds) Universitetsforlaget, Oslo (1975). (Scand J Immunol vol 2, suppl 1)
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Communicated by M.M. Green
This work was supported by PHS grant GM 23736 to V. Finnerty
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Warner, C.K., Finnerty, V. Molybdenum hydroxylases in Drosophila . Molec. Gen. Genet. 184, 92–96 (1981). https://doi.org/10.1007/BF00271201
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DOI: https://doi.org/10.1007/BF00271201