title: Alterations at the 3'-CCA end of Escherichia coli and Thermus thermophilus tRNA(Phe) do not abolish their acceptor activity.
abstract: 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.
authors.affiliation: Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk.
authors.forename: N A
authors.initials: NA
authors.lastname: Moor
authors.forename: M N
authors.initials: MN
authors.lastname: Repkova
authors.forename: V I
authors.initials: VI
authors.lastname: Yamkovoy
authors.forename: O I
authors.initials: OI
authors.lastname: Lavrik
mesh_terms: 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*
chemical_list: D012360:RNA, Transfer, Phe; D010652:Phenylalanine-tRNA Ligase