The interaction of glycyl-L-phenylalanine with the phenylalanyl-tRNA synthetase from Escherichia coli has been studied by the attempted enzymatic acylation of tRNA with the dipeptide and with the dipeptidyl-AMP anhydride. Also measured were inhibition of the formation of phenylalanyl-tRNAphe in the presence of glycyl-L-phenylalanine and the dipeptidyl-AMP analog, glycyl-L-phenylalaninol-AMP, as well as the inhibition of ATP-PP; exchange in the presence of certain amino alcohol-AMP analogs of aminoacyl adenylates. The results, which indicated specific recognition of the dipeptide and dipeptidyl-AMP anhydride by the phenylalanyl-tRNA synthetase, are of interest in terms of the mechanism by which preexisting proteins are excluded from incorporation onto tRNA.
|Original language||English (US)|
|Number of pages||9|
|State||Published - Nov 1 1974|
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