Abstract
The role of N-formyl-Met-tRNA in the intial step of protein synthesis has been examined. The formyl-accepting species of Met-tRNA, prior to its formylation, efficiently recognizes the methionine codon ApUpG in appropriate phase. Formylation reduces the efficiency of this interaction, perhaps through an alteration of secondary structure of Met-tRNA, for it also alters the mobility of Met-tRNA on a MAS column. Formylation of Met-tRNA following binding of this compound to the messenger-ribosome complex has also been demonstrated. A reaction sequence is suggested in which free Met-tRNA selects the initiator codon in complex with the ribosome, is formylated and subsequently interacts with the penultimate AA-tRNA to form the initial peptlde bond.

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