Translation of Procollagen Messenger RNA in a Cell Free System Derived from Wheat Germ: Hydroxylation of Prolyl Residues in the Product

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Abstract
Ribonucleic acid extracted from chick embryo calvaria directs the synthesis of a collagenous product in a cell free system. A portion of the prolyl residues incorporated into this protein can be hydroxylated in vitro by prolyl hydroxylase as demonstrated by the release of 3H-H2O from 3H-proline and by the direct demonstratio of 3H-hydroxyproline in acid hydrolysates of the product. Thirty percent of potential sites become hydroxy ated in the in vitro reaction using either cell-free product or an underhydroxylated collagen extracted from chick calvaria. Neither prolonged incubation nor increased levels of enzyme increased the extent of hydroxy ation in either substrate.