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大肠杆菌3'-末端16S rRNA序列在翻译过程中调节保真度。

Escherichia coli 3'-terminal 16S rRNA sequence modulated fidelity during translation.

作者信息

Latif F A, Schaup H W

机构信息

Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331.

出版信息

Biochimie. 1988 Dec;70(12):1831-9. doi: 10.1016/0300-9084(88)90045-4.

Abstract

The ribosome is a central component of the protein synthetic apparatus. Although progress has been made in characterizing the functional role of many of the ribosomal proteins, the properties of ribosomal RNA and its role in ribosome structure and function are not well understood. To investigate the working properties of the highly conserved 3'-end of 16S rRNA, a site-specific deletion was made directly within the 16S rRNA molecule. The terminal deletion did not impair in vitro 30S subunit assembly, but the particles produced lost translational fidelity in an in vitro translation system primed with natural mRNA.

摘要

核糖体是蛋白质合成装置的核心组成部分。尽管在表征许多核糖体蛋白的功能作用方面已取得进展,但核糖体RNA的特性及其在核糖体结构和功能中的作用仍未得到充分了解。为了研究16S rRNA高度保守的3'末端的工作特性,直接在16S rRNA分子内进行了位点特异性缺失。末端缺失并不损害体外30S亚基的组装,但所产生的颗粒在用天然mRNA引发的体外翻译系统中失去了翻译保真度。

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