AMINOACYL-TERT-RNA SYNTHETASE-INDUCED CLEAVAGE OF TERT-RNA

被引：20

作者：

BERESTEN, S ^{[1
]}

JAHN, M ^{[1
]}

SOLL, D ^{[1
]}

机构：

[1] YALE UNIV,DEPT MOLEC BIOPHYS & BIOCHEM,POB 6666,NEW HAVEN,CT 06511

来源：

NUCLEIC ACIDS RESEARCH | 1992年 / 20卷 / 07期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1093/nar/20.7.1523

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：

Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutaminyl-tRNA synthetase destabilizes tRNA(Gln) causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNA(Gln) species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.

引用

页码：1523 / 1530

页数：8

共 34 条

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