大肠杆菌和嗜热栖热菌苯丙氨酸tRNA在3'-CCA末端的改变不会消除它们的受体活性。

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

作者信息

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

机构信息

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

出版信息

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

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

PMID:8082771

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.

摘要

通过对大肠杆菌和嗜热栖热菌的tRNA（Phe）的3'-CCA末端进行逐步降解，随后与寡核糖核苷酸连接，将其3'-CCA末端分别变为AAA、CCC、UUU和UUA。结果显示，tRNA（UUAPhe）和tRNA（CCCPhe）在tRNA氨基酰化中具有底物活性。tRNA（AAAPhe）对大肠杆菌和嗜热栖热菌的苯丙氨酰-tRNA合成酶而言是不良底物。tRNA（UUUPhe）在tRNA氨基酰化中未检测到活性。因此，tRNA（Phe）3'-末端的性质在tRNA结合及其底物效率中起着重要作用。然而，tRNA（Phe）3'-末端的CCA序列似乎并非tRNA氨基酰化的绝对必需条件。