Alterations at the 3'-CCA end of Escherichia coli and Thermus thermophilus tRNA(Phe) do not abolish their acceptor activity.
The 3'-CCA end of tRNA(Phe) 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 tRNA(Phe) followed by the ligation with oligoribonucleotides. Substrate activity of tRNA(UUAPhe) and tRNA(CCCPhe) in tRNA aminoacylation was shown. tRNA(AAAPhe) is a bad substrate for E. coli and Th. thermophilus phenylalanyl-tRNA synthetases. tRNA(UUUPhe) has no detectable activity in tRNA aminoacylation. Therefore the nature of the 3'-end of tRNA(Phe) plays an important role in tRNA binding and its substrate efficiency. Nevertheless the CCA sequence at the 3'-end of tRNA(Phe) does not seem to be an absolute requirement for tRNA aminoacylation.
Moor
N A
NA
Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk.
Repkova
M N
MN
Yamkovoy
V I
VI
Lavrik
O I
OI
D004926:Escherichia coli / Q000201:enzymology*; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000378:metabolism*; D013379:Substrate Specificity; D016963:Thermus thermophilus / Q000201:enzymology*
D012360:RNA, Transfer, Phe; D010652:Phenylalanine-tRNA Ligase