A novel ancestral protein of Drosophila alcohol dehydrogenase in Streptomyces?
Polyclonal antibodies raised against purified Drosophila alcohol dehydrogenase (ADH) were used in Western blot analyses to search for structurally and/or immunologically related proteins in prokaryotes and eukaryotes. No immunological-reactive protein was detected in a flesh fly, a locust, and butterflies. Immunological similarity with the 50-kDa PQQ-glucose dehydrogenase (GluDH)-B enzyme of Acinetobacter calcoaceticus was found, but the cross-reactivity apparently is dependent on the high hydrophilic character of this protein. Antibodies against PQQ-GluDH did not recognize Drosophila ADH. In five of seven species of the gram-positive soil bacteria actinomycetes tested, a protein approximately 28-30 kDa in subunit size was strongly recognized by alpha-DADH. It is probably not one of the two proteins with known homology to Drosophila ADH, viz., the actIII gene product and 20 beta-hydroxysteroid dehydrogenase. The protein is present in both the soluble and the pellet-membrane fraction of the cells. The protein has a late temporal expression in surface-grown cultures and, therefore, might be involved in secondary metabolism.
Freriksen
A
A
Department of Plant Ecology and Evolutionary Biology, University of Utrecht, The Netherlands.
Heinstra
P W
PW
D000426:Alcohol Dehydrogenase / Q000235:genetics* / Q000276:immunology; D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology; D015153:Blotting, Western; D003429:Cross Reactions; D004330:Drosophila / Q000201:enzymology*; D000939:Epitopes / Q000235:genetics; D007313:Insecta / Q000201:enzymology; D013302:Streptomyces / Q000201:enzymology*
D001426:Bacterial Proteins; D000939:Epitopes; D000426:Alcohol Dehydrogenase