Alterations at the 3′‐CCA end of Escherichia coli and Thermus thermophilus tRNAPhe do not abolish their acceptor activity

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Abstract
The 3′-CCA end of tRNAPhe from Escherichia coli and Thermus thermophilus was changed to AAA, CCC, UUU and UUA by the stepwise degradation procedure of the 3′-CCA end of tRNAPhe followed by the ligation with oligoribotrinucleotides. Substrate activity of tRNAUPhe UUA and tRNAPhe CCC in tRNA aminoacylation was shown. tRNAPhe AAA is a bad substrate for E. coli and Th. thermophilus phenylalanyl-tRNA synthetases. tRNAPhe UUU has no detectable activity in tRNA aminoacylation. Therefore the nature of the 3′-end of tRNAPhe plays an important role in tRNA binding and its substrate efficiency. Nevertheless the CCA sequence at the 3′-end of tRNAPhe does not seem to be an absolute requirement for tRNA aminoacylation.