Abstract
Poly(A)-RNAs enriched for glycinin coding sequences were injected into frog oocytes and translated in the presence of either [3H]leucine or [3H]isoleucine. Sodium dodecyl sulfate electrophoresis indicated that radioactive proteins similar in size to the authentic acidic and basic polypeptide components of glycinin were not present among the glycinin-related proteins synthesized. Instead, high molecular weight precursors (Mr = 58,000-67,000) were immunoprecipitated. Unlike disulfide-linked native glycinin complexes which were cleaved by disulfide reduction, products purified from either rabbit reticulocyte lysate or oocyte translation systems were insensitive to reducing agents. The glycinin-related proteins synthesized in the oocyte were 1000 to 2000 daltons smaller than those synthesized in the reticulocyte lysate system. This result, which suggested that the oocyte system had removed NH2-terminal leader sequences of the preglycinin polypeptides, was confirmed by NH2-terminal sequence analysis of proteins synthesized in oocytes. Radioactive label was found exactly at the positions predicted by the NH2-terminal sequences of the acidic polypeptide component of native glycinin. Glycinin precursors, therefore, have an NH2-terminal leader sequence followed by the acidic peptide component and then the basic polypeptide component, joined in peptide linkage.
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