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

FEBS Letters

Lavrik, O.I.¹  Yamkovoy, V.I.²  Repkova, M.N.¹  Moor, N.A.¹ 

[1] Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Prospekt Lavrentiev 8, 630090, Novosibirsk, Russian Federation;Novosibirsk State University, 630090, Novosibirsk, Russian Federation

关键词: tRNA recognition;    3′-CCA end;    Mechanism of RNA aminoacylation;    FRS;    phenylalanyl-tRNA synthetase (E.C. 6.1.1.20);    tRNAPhe;    transfer ribonucleic acid specific to phenylalanine;    DTT;    dithiothreithol;    DS-Na;    sodium dodecyl-sulfate;   

DOI  :  10.1016/0014-5793(94)00841-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 oligoribotrinucleotides. Substrate activity of tRNAU^Phe _UUA and tRNA^Phe _CCC in tRNA aminoacylation was shown. tRNA^Phe _AAA is a bad substrate for E. coli and Th. thermophilus phenylalanyl-tRNA synthetases. tRNA^Phe _UUU 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.

【 授权许可】

Unknown