Adaptation ofDrosophilaenzymes to temperature IV. Natural selection at the alcohol-dehydrogenase locus

✍ Scribed by S. N. Alahiotis

• Publisher: Springer Netherlands
• Year: 1982
• Tongue: English
• Weight: 549 KB
• Volume: 59
• Category: Article
• ISSN: 0016-6707
• DOI: 10.1007/bf00133290

✦ Synopsis

Studies were carried out on the temperature-dependent kinetic properties (K,, Ql,,, E,, thermostability) of alcohol-dehydrogenase allozymes from D. melanogaster. It was shown that there is a parallelism between the biochemical properties of the enzymes and the behaviour of the genes in natural and cage populations. Furthermore, the relationship between the temperature-dependent kinetic properties of alcohol dehydrogenase and assay temperature was examined in three tropical and two temperate Drosophila species. K, patterns were similar among species from the same habitat and different between habitats. No such parallelism was seen with respect to thermal inactivation. The Qlc values in general reflected temperature-dependent changes in K,. It is discussed that the mechanistic connection observed between the biochemical and population levels (intra-and interspecifically) strongly suggests that temperature acts as a selective factor on the structural Adh locus in the genus Drosophila.