Human tyrosine tRNA is also internally cleavable by E-coli ribonuclease P RNA ribozyme in vitro

被引：10

作者：

Ando, T ^{[1
]}

Tanaka, T ^{[1
]}

Hori, Y ^{[1
]}

Sakai, E ^{[1
]}

Kikuchi, Y ^{[1
]}

机构：

[1] Toyohashi Univ Technol, Dept Ecol Engn, Div Biosci & Biotechnol, Toyohashi, Aichi 4418580, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2001年 / 65卷 / 12期

关键词：

Escherichia coli; tRNA; RNase P; hyperprocessing; tyrosine;

D O I：

10.1271/bbb.65.2798

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Transfer RNA is an essential molecule for biological system, and each tRNA molecule commonly has a cloverleaf structure. Previously, we experimentally showed that some Drosophila tRNA (tRNA(Ala), tRNA(His), and tRNA(i)(Met)) molecules fit to form another, non-cloverleaf, structure in which the 3'-half of the tRNA molecules forms an alternative hairpin, and that the tRNA molecules are internally cleaved by the catalytic RNA of bacterial ribonuclease P (RNase P). Until now, the hyperprocessing reaction of tRNA has only been reported with Drosophila tRNAs. This time, we applied the hyperprocessing reaction to one of human tRNAs, human tyrosine tRNA, and we showed that this tRNA was also hyperprocessed by E. coli RNase P RNA. This tRNA is the first example for hyperprocessed non-Drosophila tRNAs. The results suggest that the hyperprocessing reaction can be a useful tool to detect destablized tRNA molecules from any species.

引用

页码：2798 / 2801

页数：4

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