tRNA^Phe deprived of 3′‐terminal adenosyl residue does not stimulate adenosine aminoacylation catalysed by phenylalanyl‐tRNA synthetase from Escherichia coli

Abstract

Phenylalanyl‐tRNA synthetase from Escherichia coli does not catalyze the [14C]phenylalanyl residue transfer from phenylalanyl‐adenylate to adenosine either in the presence or absence of homologous tRNAPhe and tRNAPhe −A. When the reaction mixture contained dithiothreitol, radioactive substance was detected having a mobility on HPLC column close to that of aminoacyladenosine. The amount of this product depended on the concentration of dithiothreitol in the mixture. Phenylalanyl residue was suggested to undergo transfer from aminoacyladenylate to dithiothreitol molecule.