Developmental and evolutionary comparisons of proteins from purified ribosomal subunits in two silkmoths.

Developmental comparisons of silkmoth ribosomal proteins were performed by parallel two-dimensional electrophoretic analyses of proteins derived from developing adult wings and from ovarian follicles at the prechoriogenic and choriogenic stages of development (before and during secretion of the chorion, respectively). Proteins of 40S and 60S subunits were prepared and analyzed separately. A single major developmental difference was observed, exclusively in choriogenic follicles: the majority of a 40S subunit protein, S6, was shifted to a more acidic form, possibly as a result of phosphorylation. A less prominent change was apparently due to quantitative variation between two forms of one large subunit protein. The developmental comparisons were performed in two species of the genus Antheraea, with consistent results. Comparisons between the two species revealed remarkable evolutionary conservation of the ribosomal protein patterns, sharply contrasting with the evolutionary diversification of chorion structural proteins in the same two species. The only detectable interspecies differences in ribosomal components were (a) slightly more acidic behaviour of one small-subunit protein and more basic behaviour of one large-subunit protein in Antheraea polyphemus as compared to Antheraea pernyi, and (b) presence of an apparently species-specific 60 S subunit protein in A. pernyi, which in A. polyphemus probably co-migrates with a neighbouring protein.