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对四膜虫核酶内取代P5abc的新构建结构域的表征。

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

作者信息

Ikawa Y, Shiraishi H, Inoue T

机构信息

Department of Chemistry, Faculty of Science, Kyoto University, Japan.

出版信息

FEBS Lett. 1996 Sep 23;394(1):5-8. doi: 10.1016/0014-5793(96)00918-0.

Abstract

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.

摘要

嗜热四膜虫核酶的P5abc结构域已被证明可作为激活剂,增强核酶的核心催化活性。我们之前报道过,一些一级序列与P5abc不同的新结构域也能够激活核酶。尚不清楚新结构域的激活机制是否与P5abc相同。我们研究了这些新结构域的结构和功能特性,并获得了有力证据,表明特定结构域以与P5abc不同的方式激活核酶。

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