Translation of collagen messenger RNA in a cell-free system derived from wheat germ.
A cell-free system for synthesizing protein from wheat germ was used to translate the messenger RNA extracted from 16-day embryonic chick calvaria. A part of the product had properties similar to collagenous peptides and served as a substrate for prolyl hydroxylase, an enzyme specific for collagen. The level of potassium was critical for the synthesis of high molecular weight products with properties similar to pro-alpha-chains. The potassium concentration for optimal protein synthesis, as judged by maximum incorporation of [3H]proline into acid precipitable material, was considerably lower than the concentration required for the synthesis of high molecular weight collagenous peptides.
D000818:Animals; D002474:Cell-Free System; D002642:Chick Embryo; D003094:Collagen / Q000096:biosynthesis*; D003012:Microbial Collagenase; D009994:Osmolar Concentration; D010452:Peptide Biosynthesis; D011188:Potassium / Q000494:pharmacology; D011393:Procollagen-Proline Dioxygenase / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D014908:Triticum / Q000378:metabolism*
D012333:RNA, Messenger; D003094:Collagen; D011393:Procollagen-Proline Dioxygenase; D003012:Microbial Collagenase; D011188:Potassium