Alcohol Dehydrogenase Gene of Drosophila melanogaster: Relationship of Intervening Sequences to Functional Domains in the Protein

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 78; no. 5; pp. 2717 - 2721
• Main Authors: Benyajati, Cheeptip, Place, Allen R., Powers, Dennis A., Sofer, William
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 01-05-1981; National Acad Sciences
• Subjects: Alcohol Dehydrogenase; Alcohol Oxidoreductases - genetics; Amino Acid Sequence; Amino acids; Animals; Base Sequence; Circular Dichroism; Cloning, Molecular; Codon - genetics; Codons; Coenzymes; Dehydrogenases; DNA; DNA, Recombinant - metabolism; Drosophila; Drosophila melanogaster - enzymology; Drosophila melanogaster - genetics; Enzymes; Genes; Genetic Code; Introns; Nucleotide sequences; Nucleotides; Protein Conformation
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.78.5.2717

The gene that codes for Drosophila alcohol dehydrogenase (ADH; alcohol: NAD+oxidoreductase, EC 1.1.1.1) was identified in a bacteriophage λ library of genomic Drosophila DNA by using ADH cDNA cloned DNA as a probe. The DNA sequence of the protein encoding region was shown to be in agreement with the amino acid sequence of the ADH. Two intervening DNA sequences (introns) were identified within the protein encoding region: one was 65 nucleotides and located between the codons for amino acid residues 32 and 33, and one was 70 nucleotides and located between the codons for amino acid residues 167 and 168. Both contained the 5′G-T and 3′A-G dinucleotides characteristic of intron boundaries of eukaryotic genes. On the basis of secondary structure predictions, the first 140 amino acid residues of Drosophila ADH are in an alternating β -sheet/α -helix arrangement which is characteristic of the coenzyme binding domain of dehydrogenases. The smaller of the two introns interrupts the domain predicted to bind the adenine portion of the coenzyme.