Alterations at the 3'-CCA end of Escherichia coli and Thermus thermophilus tRNA(Phe) do not abolish their acceptor activity

N A Moor; M N Repkova; V I Yamkovoy; O I Lavrik

doi:10.1016/0014-5793(94)00841-8

Alterations at the 3'-CCA end of Escherichia coli and Thermus thermophilus tRNA(Phe) do not abolish their acceptor activity

FEBS Lett. 1994 Sep 5;351(2):241-2. doi: 10.1016/0014-5793(94)00841-8.

Authors

N A Moor¹, M N Repkova, V I Yamkovoy, O I Lavrik

Affiliation

¹ Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk.

PMID: 8082771
DOI: 10.1016/0014-5793(94)00841-8

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.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Escherichia coli / enzymology*
Phenylalanine-tRNA Ligase / metabolism*
RNA, Transfer, Phe / metabolism*
Substrate Specificity
Thermus thermophilus / enzymology*

Substances

RNA, Transfer, Phe
Phenylalanine-tRNA Ligase