Synthesis of the crystalloid protein complex in vivo in the endosperm of developing castor bean seeds.

The synthesis of subunit polypeptides of the crystalloid protein complex has been examined in endosperm from developing castor bean (Ricinus communis L. cv Hale) seeds. Pulse-label and -chase studies in vivo have shown that synthesis initially involves the formation of high molecular weight precursors (50 to 60 kilodaltons) comprising peptide-linked acidic and basic polypeptides. Precursor processing involves the posttranslational cleavage of the peptide bond to yield authentic and polypeptides. This processing has a half-life of 35 to 40 minutes and is preceded by a 45- to 60-minute lag period. Both precursor and subunit polypeptides are shown to exhibit similar molecular weight and pI heterogeneity, and this is suggested to be due to the expression of a multigene family.