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Biochem J. Nov 15, 2002; 368(Pt 1): 333–340.
PMCID: PMC1222967

Identification of Drosophila melanogaster yellow-f and yellow-f2 proteins as dopachrome-conversion enzymes.

Abstract

This study describes the identification of Drosophila yellow-f and yellow-f2 as dopachrome-conversion enzymes responsible for catalysing the conversion of dopachrome into 5,6-dihydroxyindole in the melanization pathway. Drosophila yellow -y gene and yellow -b, -c, -f and -f2 genes were expressed in an insect cell/baculovirus expression system and their corresponding recombinant proteins were screened for dopachrome-conversion enzyme activity. Among the yellow and yellow -related genes, the yellow -f and yellow -f2 genes were identified as the genes coding for Drosophila dopachrome-conversion enzyme based on the high activity of their recombinant proteins in catalysing the production of 5,6-dihydroxyindole from dopachrome. Both yellow-f and yellow-f2 are capable of mediating a decarboxylative structural rearrangement of dopachrome, as well as an isomerization/tautomerization of dopamine chrome and dopa methyl ester chrome. Northern hybridization revealed the transcription of yellow -f in larvae and pupae, but a high abundance of mRNA was observed in later larval and early pupal stages. In contrast, yellow-f2 transcripts were present at all stages, but high abundance of its mRNA was observed in later-stage pupae and adults. These data indicate that yellow-f and yellow-f2 complement each other during Drosophila development and that the yellow-f is involved in larval and pupal melanization, and yellow-f2 plays a major role in melanization reactions in Drosophila during later pupal and adult development. Results from this study provide the groundwork towards a better understanding of the physiological roles of the Drosophila yellow gene family.

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Selected References

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  • Cherqui A, Duvic B, Reibel C, Brehélin M. Cooperation of dopachrome conversion factor with phenoloxidase in the eumelanin pathway in haemolymph of Locusta migratoria (Insecta). Insect Biochem Mol Biol. 1998 Nov;28(11):839–848. [PubMed]
  • Sugumaran M, Semensi V. Quinone methide as a new intermediate in eumelanin biosynthesis. J Biol Chem. 1991 Apr 5;266(10):6073–6078. [PubMed]
  • Li J, Nappi AJ. Electrochemical identification of dopachrome isomerase in Drosophila melanogaster. Biochem Biophys Res Commun. 1991 Oct 31;180(2):724–729. [PubMed]
  • Johnson JK, Li J, Christensen BM. Cloning and characterization of a dopachrome conversion enzyme from the yellow fever mosquito, Aedes aegypti. Insect Biochem Mol Biol. 2001 Oct;31(11):1125–1135. [PubMed]
  • Fang Jianmin, Han Qian, Johnson Jody K, Christensen Bruce M, Li Jianyong. Functional expression and characterization of Aedes aegypti dopachrome conversion enzyme. Biochem Biophys Res Commun. 2002 Jan 11;290(1):287–293. [PMC free article] [PubMed]
  • Barber JI, Townsend D, Olds DP, King RA. Dopachrome oxidoreductase: a new enzyme in the pigment pathway. J Invest Dermatol. 1984 Aug;83(2):145–149. [PubMed]
  • Leonard LJ, Townsend D, King RA. Function of dopachrome oxidoreductase and metal ions in dopachrome conversion in the eumelanin pathway. Biochemistry. 1988 Aug 9;27(16):6156–6159. [PubMed]
  • Pawelek JM. Dopachrome conversion factor functions as an isomerase. Biochem Biophys Res Commun. 1990 Feb 14;166(3):1328–1333. [PubMed]
  • Aroca P, Garcia-Borron JC, Solano F, Lozano JA. Regulation of mammalian melanogenesis. I: Partial purification and characterization of a dopachrome converting factor: dopachrome tautomerase. Biochim Biophys Acta. 1990 Sep 14;1035(3):266–275. [PubMed]
  • Aroca P, Solano F, Salinas C, García-Borrón JC, Lozano JA. Regulation of the final phase of mammalian melanogenesis. The role of dopachrome tautomerase and the ratio between 5,6-dihydroxyindole-2-carboxylic acid and 5,6-dihydroxyindole. Eur J Biochem. 1992 Aug 15;208(1):155–163. [PubMed]
  • Tsukamoto K, Jackson IJ, Urabe K, Montague PM, Hearing VJ. A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme termed DOPAchrome tautomerase. EMBO J. 1992 Feb;11(2):519–526. [PMC free article] [PubMed]
  • Solano F, Jiménez-Cervantes C, Martínez-Liarte JH, García-Borrón JC, Jara JR, Lozano JA. Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome tautomerase. Biochem J. 1996 Jan 15;313(Pt 2):447–453. [PMC free article] [PubMed]
  • Biessmann H. Molecular analysis of the yellow gene (y) region of Drosophila melanogaster. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7369–7373. [PMC free article] [PubMed]
  • Geyer PK, Corces VG. Separate regulatory elements are responsible for the complex pattern of tissue-specific and developmental transcription of the yellow locus in Drosophila melanogaster. Genes Dev. 1987 Nov;1(9):996–1004. [PubMed]
  • Drapeau MD. The Family of Yellow-Related Drosophila melanogaster Proteins. Biochem Biophys Res Commun. 2001 Mar 2;281(3):611–613. [PubMed]
  • Albert S, Bhattacharya D, Klaudiny J, Schmitzová J, Simúth J. The family of major royal jelly proteins and its evolution. J Mol Evol. 1999 Aug;49(2):290–297. [PubMed]
  • Schmitzová J, Klaudiny J, Albert S, Schröder W, Schreckengost W, Hanes J, Júdová J, Simúth J. A family of major royal jelly proteins of the honeybee Apis mellifera L. Cell Mol Life Sci. 1998 Sep;54(9):1020–1030. [PubMed]
  • Albert S, Klaudiny J, Simúth J. Molecular characterization of MRJP3, highly polymorphic protein of honeybee (Apis mellifera) royal jelly. Insect Biochem Mol Biol. 1999 May;29(5):427–434. [PubMed]
  • Charlab R, Valenzuela JG, Rowton ED, Ribeiro JM. Toward an understanding of the biochemical and pharmacological complexity of the saliva of a hematophagous sand fly Lutzomyia longipalpis. Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):15155–15160. [PMC free article] [PubMed]
  • Valenzuela JG, Belkaid Y, Garfield MK, Mendez S, Kamhawi S, Rowton ED, Sacks DL, Ribeiro JM. Toward a defined anti-Leishmania vaccine targeting vector antigens: characterization of a protective salivary protein. J Exp Med. 2001 Aug 6;194(3):331–342. [PMC free article] [PubMed]
  • Wittkopp Patricia J, True John R, Carroll Sean B. Reciprocal functions of the Drosophila yellow and ebony proteins in the development and evolution of pigment patterns. Development. 2002 Apr;129(8):1849–1858. [PubMed]
  • Wakamatsu K, Ito S. Preparation of eumelanin-related metabolites 5,6-dihydroxyindole, 5,6-dihydroxyindole-2-carboxylic acid, and their O-methyl derivatives. Anal Biochem. 1988 May 1;170(2):335–340. [PubMed]
  • Sugumaran Manickam. Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell Res. 2002 Feb;15(1):2–9. [PubMed]
  • Li J. Egg chorion tanning in Aedes aegypti mosquito. Comp Biochem Physiol A Physiol. 1994 Dec;109(4):835–843. [PubMed]

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