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

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Abstract
Developmental comparisons of silkmoth ribosomal proteins were performed by parallel 2-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 40 S and 60 S subunits were prepared and analyzed separately. A single major developmental difference was observed, exclusively in choriogenic follicles: the majority of a 40 S 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 2 forms of 1 large subunit protein. The developmental comparisons were performed for Antheraea polyphemus and A. pernyi with consistent results. Comparisons between the 2 spp. revealed remarkable evolutionary conservation of the ribosomal protein patterns, sharply contrasting with the evolutionary diversification of their chorion structural proteins. The only detectable interspecies differences in ribosomal components were slightly more acidic behavior of 1 small-subunit protein and more basic behavior of 1 large-subunit protein in A. polyphemus as compared to A. pernyi, and presence of an apparently species-specific 60 S subunit protein in A. pernyi, which in A. polyphemus probably co-migrates with a neighboring protein.