Structural Characterization of the α -glycerol-3-phosphate Dehydrogenase-Encoding Gene of Drosophila melanogaster

• Published in: Proceedings of the National Academy of Sciences - PNAS 1989-07, Vol.86 (13), p.5020-5024
• Main Authors: Von Kalm, Laurence, Weaver, Jonna, DeMarco, Judy, MacIntyre, Ross J., Sullivan, David T.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Animals; Base Sequence; Biological and medical sciences; Cloning, Molecular; Complementary DNA; Diptera; DNA; Drosophila; Drosophila melanogaster - enzymology; Drosophila melanogaster - genetics; Drosophilidae; Exons; Fundamental and applied biological sciences. Psychology; Genes; Genes. Genome; Genomics; Glycerolphosphate Dehydrogenase - genetics; Larvae; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Protein isoforms; RNA; RNA, Messenger - genetics; Transcription, Genetic
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.13.5020

In Drosophila, multiple isoforms of α -glycerol-3-phosphate dehydrogenase (sn-glycerol-3-phosphate: NAD+2-oxidoreductase, EC 1.1.1.8) are produced in a tissue-and stage-specific manner. To understand the underlying molecular basis of these isoforms, we have sequenced a 5.8-kilobase region of the Drosophila genome that contains the entire Gpdh locus. Primer-extension and RNase protection assays show that the gene consists of eight exons and has a single transcription-start point. RNase protection mapping and comparison of the genomic sequence from three different cDNA clones reveal that three protein isoforms of glycerol-3-phosphate dehydrogenase are produced by alternative processing of 3′exons. Two of the isoforms differ from the third by the addition of either three or ten amino acids to their C-terminal ends. Transcripts corresponding to two of the isoforms are expressed during both larval and adult stages, while the third isoform is produced only in adults.