Characterization of Two Alcohol Dehydrogenase (Adh) Loci from the Olive Fruit Fly, Bactrocera (Dacus) oleae and Implications for Adh Duplication in Dipteran Insects

Abstract

We report the cloning and structural characterization of two Adh loci of the olive fruit fly, Bactrocera oleae. Each of the two genes, named Adh1 and Adh2, consists of three exons and two introns for a total length of 1981 and 988 nucleotides, respectively. Their deduced amino acid sequences of 257 and 258 residues exhibit a 77% identity and display the characteristics of the insect ADH enzymes, which belong to the short-chain dehydrogenases/reductases family. The Adh genes of B. oleae are compared to the two genes of the Mediterranean fly, Ceratitis capitata, the only other species of the Tephritidae family in which the Adh genes have been studied. On the basis of amino acid divergence the four genes form two clusters each containing one gene from each species, as expected if there was one duplication event before speciation. On the basis of nucleotide sequence the four sequences form two clusters each containing the two sequences from the same species, as expected if there was a separate duplication event in each species. To help decide between the two alternatives, we compared at both the amino acid and DNA level the Adh genes of five Drosophila species that are known to carry two such genes and observed that, with only one exception at the amino acid level, conspecific loci cluster together. We conclude that the information we have at present does not allow a firm choice between the hypothesis of a single duplication event that occurred before the split of Bactrocera and Ceratitis from their common ancestor and the hypothesis of two independent duplication events, one in each of the two genera.

Genomic organization and functional characterization of the alcohol dehydrogenase locus of Ceratitis capitata (Medfly)

“…Recently, the cDNA encoding for ADH was cloned and sequenced in several species outside Drosophilidae: Sarcophaga peregrina (Horio et al ., 1996), Bactrocera oleae (Benos et al . 2000; Goulielmos et al ., 2001, 2003a), B . cucurbitae , B .…”

“…Recently, the cDNA encoding for ADH was cloned and sequenced in several species outside Drosophilidae: Sarcophaga peregrina (Horio et al ., 1996), Bactrocera oleae (Benos et al . 2000;Goulielmos et al ., 2001Goulielmos et al ., , 2003a (Goulielmos et al ., 2003b), Ceratitis capitata (Brogna et al ., 2001), C. cosyra , C. rosa and C. fasciventris (Goulielmos et al ., 2003b). The species of the genera Ceratitis and Bactrocera belong to the family Tephritidae, which is relatively close to Drosophilidae (both families belong to the subsection Acalyptratae of the infraorder Brachycera).…”

Tracing the History of an Enzyme Polymorphism: The Case of Alcohol Dehydrogenase-2 (Adh-2) of the Olive Fruit Fly Bactrocera oleae

“…The latter hypothesis has also been suggested for the glycerol-3-phosphate dehydrogenase of Drosophila (Kwiatowski et al 1997). Goulielmos et al (2001) have shown that Bactrocra oleae has also a duplicate Adh system and obtained the full genomic sequence of these loci. By making use of the available information on cDNA sequences from the medfly, they attempted to answer the question of whether in tephritids a single prespeciation duplication event is a more likely alternative to the hypothesis of two separate postspeciation duplication events.…”

Effect of acetone feeding on alcohol dehydrogenase activity in the olive fruit fly, Bactrocera oleae

“…Further examination showed that in colonies of the olive fruit fly B. oleae, originating from several independent populations and maintained on an artificial substrate, the ADH-I allele of the ADH locus, whose frequency in natural populations is less than 1%, rises in frequency to about 30% within four generations of artificial rearing, that of ADH-S, which is most common in natural populations, suffers a compensatory decrease from 60% to 30% whereas that of ADH-F is only slightly affected. Since then, a considerable amount of information about the ADH locus has been obtained (Cosmides et al, 1997;Cosmidis et al, 1999;Mazi et al, 1998b;Benos et al, 2000;Goulielmos et al, 2001). The B. oleae ADH selection pressure appears to be amongst the largest ever reported for allozymes, and is only comparable to selection pressure suffered by plants growing on soils contaminated by heavy metals (Jain and Bradshaw, 1966).…”