Molecular and biochemical characterization of the aaNAT1 (Dat) locus in Drosophila melanogaster: differential expression of two gene products.

Brodbeck, D; Amherd, R; Callaerts, P; Hintermann, E; Meyer, U A; Affolter, M

Brodbeck, D; Amherd, R; Callaerts, P; Hintermann, E; Meyer, U A; Affolter, M.

Afiliación

Brodbeck D; Department of Pharmacology, Biozentrum of the University of Basel, Switzerland.

DNA Cell Biol ; 17(7): 621-33, 1998 Jul.

Article en En | MEDLINE | ID: mdl-9703021

RESUMEN

In insects, arylalkylamine N-acetyltransferases (AANATs) have been implicated in several physiological processes, including sclerotization, inactivation of certain neurotransmitters, and, similar to the function in vertebrates, catalysis of the rate-limiting step in melatonin biosynthesis. Here, we report an extensive biochemical and functional analysis of the products of the aaNAT1 gene of Drosophila melanogaster. The aaNAT1 gene generates two transcripts through alternative first-exon usage. These transcripts are under tissue-specific and developmental control and encode proteins which differ in their N-terminus with respect to their starting methionine. The more abundant isoform, AANATlb, is first expressed during late embryogenesis in the brain, the ventral nerve cord, and the midgut; in adults, AANATlb is still detectable in the brain and midgut. The less abundant isoform, AANATla, appears only during late pupal stages and in adults is found predominantly in the brain. We demonstrate that the mutation Dat(lo) represents a hypomorphic allele of aaNAT1b, in which an insertion of two transposable elements, MDG412 and blastopia, has occurred within the first intron of the gene. Using a deficiency which removes the aaNAT1 gene, we provide evidence that aaNAT1 is not essential for the process of sclerotization. Furthermore, neither of the two enzyme isoforms shows circadian regulation of RNA or protein levels. The differing levels of abundance and distinct developmental control of AANAT1a and AANAT1b suggest different in vivo functions for these two enzymes.

Asunto(s)

Arilamina N-Acetiltransferasa/genética; Drosophila melanogaster/genética; Genes de Insecto/genética; Empalme Alternativo/genética; Animales; Arilamina N-Acetiltransferasa/química; Arilamina N-Acetiltransferasa/metabolismo; Encéfalo/embriología; Encéfalo/enzimología; Ritmo Circadiano/genética; Clonación Molecular; Elementos Transponibles de ADN/genética; ADN Complementario/análisis; ADN Complementario/genética; Sistema Digestivo/embriología; Sistema Digestivo/enzimología; Drosophila melanogaster/enzimología; Drosophila melanogaster/fisiología; Embrión no Mamífero/enzimología; Exones/genética; Regulación del Desarrollo de la Expresión Génica; Regulación Enzimológica de la Expresión Génica; Proteínas de Insectos/genética; Proteínas de Insectos/metabolismo; Isoenzimas/química; Isoenzimas/genética; Isoenzimas/metabolismo; Mutación/genética; Sistema Nervioso/embriología; Sistema Nervioso/enzimología; ARN/análisis; ARN/genética; Análisis de Secuencia de ADN; Especificidad por Sustrato; Transcripción Genética/genética

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arilamina N-Acetiltransferasa / Genes de Insecto / Drosophila melanogaster Idioma: En Revista: DNA Cell Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 1998 Tipo del documento: Article País de afiliación: Suiza Pais de publicación: Estados Unidos

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