Phenylalanyl-tRNA Synthetase and Isoleucyl-tRNAPhe: A Possible Verification Mechanism for Aminoacyl-tRNA

摘要: Abstract The synthesis of isoleucyl-tRNAPhe (Escherichia coli) proceeds at an appreciable rate under normal in vitro conditions the presence isoleucyl-tRNA synthetase (EC 6.1.1.5) from E. coli. The misacylated product is shown here to be hydrolyzed by highly purified phenylalanyl-tRNA coli, with release isoleucine and active tRNAPhe. Thus, possesses a previously unrecognized activity, which deacylates mistakenly acylated tRNAPhe; enzyme inactive toward correctly matched aminoacyl tRNAs. Such mechanism could serve verify aminoacyl-tRNAs, deacylating those that are misacylated. common generalization needs modified: amino acid not necessarily committed given (incorrect) anticodon when it incorporated into aminoacyl-tRNA. It may possible correct thereafter.