Sequence and structure of the dopa decarboxylase gene of Drosophila: evidence for novel RNA splicing variants.
In Drosophila, dopa decarboxylase (DDC) serves a dual role in neurotransmitter production and sclerotization of the cuticle. The Ddc gene is under complex hormonal and tissue-specific control and several sizes of Ddc RNA are observed at embryonic hatching, pupariation and adult eclosion. We present here the complete nucleotide sequence of the Drosophila dopa decarboxylase gene and the partial sequence of two corresponding Ddc cDNAs. The sequence allows us to account for the detailed structure of four of the five major Ddc RNA species observed. The cDNA sequence reveals the existence of previously undetected splicing events and provides evidence for two RNA splicing alternatives which appear to encode two protein isoforms. The structure, processing and developmental regulation of the Ddc transcripts and putative protein isoforms are discussed. Interestingly, the pyridoxal-binding peptide of porcine DDC matches the Drosophila sequence perfectly suggesting considerable selective pressure on at least portions of the sequence. This is the first available Ddc gene sequence from any organism and should serve as a basis of comparison for the related proteins of other species.
D000595:Amino Acid Sequence; D000818:Animals; D001142:Aromatic-L-Amino-Acid Decarboxylases / Q000235:genetics*; D001483:Base Sequence; D004262:DNA Restriction Enzymes; D004296:Dopa Decarboxylase / Q000235:genetics*; D004330:Drosophila / Q000201:enzymology / Q000235:genetics*; D005796:Genes; D014644:Genetic Variation; D012326:RNA Splicing
D004262:DNA Restriction Enzymes; D004296:Dopa Decarboxylase; D001142:Aromatic-L-Amino-Acid Decarboxylases