Abstract
Increasing data on Drosophila alcohol dehydrogenase (ADH) sequences have made it possible to calculate the rate of amino acid replacement per year, which is 1.7 x 10(-9). This value makes this protein suitable for reconstructing phylogenetic relationships within the genus for those species for which no molecular data are available such as Scaptodrosophila. The amino acid sequence of Drosophila lebanonensis is compared to all of the already known Drosophila ADHs, stressing the unique characteristic features of this protein such as the conservation of an initiating methionine at the N-terminus, the unique replacement of a glycine by an alanine at a very conserved position in the NAD domain of all dehydrogenases, the lack of a slow-migrating peptide, and the total conservation of the maximally hydrophilic peptide. The functional significance of these features is discussed. Although the percent amino acid identity of the ADH molecule in Drosophila decreases as the number of sequences compared increases, the conservation of residue type in terms of size and hydrophobocity for the ADH molecule is shown to be very high throughout the genus Drosophila. The distance matrix and parsimony methods used to establish the phylogenetic relationships of D. lebanonensis show that the three subgenera, Scaptodrosophila, Drosophila, and Sophophora separated at approximately the same time.
