Characterization of the newly constructed domains that replace P5abc within the Tetrahymena ribozyme

被引：8

作者：

Ikawa, Y ^{[1
]}

Shiraishi, H ^{[1
]}

Inoue, T ^{[1
]}

机构：

[1] KYOTO UNIV,FAC SCI,DEPT CHEM,KYOTO 60601,JAPAN

来源：

FEBS LETTERS | 1996年 / 394卷 / 01期

关键词：

Tetrahymena; ribozyme; P5abc; gel mobility shift;

D O I：

10.1016/0014-5793(96)00918-0

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：

The P5abc domain of the Tetrahymena ribozyme has been shown to function as an activator that enhances core catalytic activity of the ribozyme. We reported previously that several new domains in that their primary sequences are different from that of P5abc are also capable of activating the ribozyme. It was unclear whether the mechanism of activation by the new domains is identical to that by P5abc. We have investigated structural and functional properties of the new domains and obtained evidence that strongly indicates that a particular domain activates the ribozyme in a different manner from that by P5abc.

引用

页码：5 / 8

页数：4

共 11 条

[1]

Ikawa Y, 1995, TRACING BIOLOGICAL EVOLUTION IN PROTEIN AND GENE STRUCTURES, P115

[2] SECONDARY STRUCTURE OF THE CIRCULAR FORM OF THE TETRAHYMENA RIBOSOMAL-RNA INTERVENING SEQUENCE - A TECHNIQUE FOR RNA STRUCTURE-ANALYSIS USING CHEMICAL PROBES AND REVERSE-TRANSCRIPTASE [J].