Vitellogenin protein diversity in the HawaiianDrosophila

Egg and female hemolymph proteins were resolved via SDS-polyacrylamide gel electrophoresis in a diverse array of 33 endemic Hawaiian drosophilids, encompassing 17 picture-winged species, 3 of theantopocerus species group, 9 fungus feeders, 1 species from each of the modified mouthparts,crassifemur and ciliated tarsus groups, and 1Scaptomyza species. Molecular weights of the two (10 species) or three vitellogenin bands (22 species) were highly variable, spanning a 7-kD range. The largest vitellogenin, V₁, was the most variable, showing a change of some 10% in its mean size of 47.6 kD. The smallest V₃ vitellogenin, mean size 44.1 kD, was evolutionarily the most conservative in size. The speciesDrosophila hawaiiensis was found to be polymorphic for two/three vitellogenin bands and, also, polymorphic with respect to the size of the V₁ protein. No inter- or intrapopulation variability in vitellogenin size was detected in 10 other species examined. The major features of vitellogenin protein evolution in the HawaiianDrosophila are change in molecular weight and regulatory differences that result in quantitative differences between species in patterns of vitellogenin protein production. This research was supported by NSF Grants DEB-7619872 and PCM-7913074. This paper is No. III in the series “Studies of Oogenesis in Natural Populations of Drosophilidae.”