Abstract
Synthesis of the three vitellogenin polypeptides (molecular weights of 44,000, 45,000, and 46,000) of Drosophila melanogaster has been analyzed in vivo and in a cell-free system. After labeling periods in vivo, the three vitellogenin polypeptides were made as the principal synthetic products of the female fat body. During a short (0.5 min) labeling period, they were identified as discrete species on two-dimensional gels. Two of the polypeptides have molecular weights of 45,000 and a third has a molecular weight of 44,000. After longer labeling periods (5-45 min) the three mature vitellogenins appeared. Both immunoprecipitation and peptide mapping confirmed that the species labeled at 0.5 min are immature forms of the vitellogenin polypeptides. In vitro translation of poly(A)-RNA from female fat body indicated another processing step in vitellogenin synthesis. Three polypeptides were obtained that were identified as precursors of the vitellogenins on the basis of immunoprecipitation and peptide mapping. Two of the translation products have a molecular weight of 46,000 and the third has a molecular weight of 45,000. Because the vitellogenins are secreted proteins, we interpret the higher molecular weight of the in vitro translation products as being due to signal peptides.