Dleb\Adhr is transcribed as a dicistronic mRNA with Dleb\Adh.

The crystal structure of Dleb\Adh protein has been determined.

The phylogenetic relationships and divergence times of 39 drosophilid species have been studied by using the coding region of the Adh gene.

The homologous genomic region containing Adh and Adhr is analysed. Ka and Ks values are determined (Ks values for Adh are significantly lower than values for Adhr) and amino acid comparisons reveal conserved regions shared by Adh and Adhr which have been assigned to known functional domains.

The D.lebanonensis genomic region containing Dleb\Adh and Dleb\Adhr has been cloned and sequenced.

Adh activity in 71 Drosophila species is assayed to determine if the protein plays a key role in the adaptation of species to substrates undergoing alcoholic fermentation.

The Adh genomic region of D.lebanonensis, which includes Dleb\Adh and Dleb\Adhr, has been cloned and sequenced, and compared with the corresponding region from D.immigrans and D.subobscura.

Adult acetic acid tolerance found to correlate with ethanol tolerance.

Phylogenetic DNA sequence comparison of ten Drosophila species has been used to elucidate the secondary structure of Adh mRNA. One possible pairing region in the 5' leader sequence and 22 in the coding and noncoding regions have been identified by seeking an equivalent pairing region in homologous RNA. Most are short range pairings such as hairpins. The rate of coevolution in noncoding pairing region is higher than in coding regions in accordance with selective constraints on substitution rates in coding region.

Phylogenetic relationships in Drosophila are studied using the Alcohol dehydrogenase locus in several species.

The functional Dleb\Adh gene product is a dimer with a monomeric Mr of 27000 and with 254 residues in each polypeptide chain. Crystals of the protein in the presence of cofactor are plate-like with varying dimensions and twinned. In the absence of cofactor crystals were monoclinic.

Dleb\Adh amino acid sequence was compared to already known Drosophila Adh genes and 10 unique amino acid replacements were found. 4 nonconservative substitutions were found at positions 33, 456, 60 and 191. At position 191 a thr is present where it is a lys in all other Drosophila dehydrogenases, this substitution is also seen in Adh^F. 6 conservative substitutions, with respect to size and hydrophobicity, are present. At position 13, in the NAD binding domain, ala not gly is present as seen in other Drosophila dehydrogenases. 62.6% amino acid identity throughout Drosophila ADH proteins. Distance matrix and parsimony methods were used to establish the phylogenetic relationship of D.lebanonensis and demonstrated that the 3 subgenera Scaptodosophila, Drosophila and Sophophora separated at approximately the same time.

In situ hybridization assays reveal a single chromosomal location of Dleb\Adh.

Dleb\Adh coding region has been sequenced.

Organization of Dleb\Adh locus has been determined.

Three Adh protein antibodies were characterized and immunoblotting assays found that they cross-react to Adh genes from D.melanogaster, D.bocqueti, D.erecta, D.teissieri and D.lebanonensis. ADH specific activity in different larval organs was found to be similar whereas protein distribution varies substantially.