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多嘧啶序列结合蛋白功能结构域的确定

Determination of functional domains in polypyrimidine-tract-binding protein.

作者信息

Oh Y L, Hahm B, Kim Y K, Lee H K, Lee J W, Song O, Tsukiyama-Kohara K, Kohara M, Nomoto A, Jang S K

机构信息

Department of Life Science, Pohang University of Science and Technology, San31, Hyoja-Dong, Pohang, Kyungbuk 790-784, South Korea.

出版信息

Biochem J. 1998 Apr 1;331 ( Pt 1)(Pt 1):169-75. doi: 10.1042/bj3310169.

Abstract

Polypyrimidine-tract-binding protein (PTB) is involved in pre-mRNA splicing and internal-ribosomal-entry-site-dependent translation. The biochemical properties of various segments of PTB were analysed in order to understand the molecular basis of the PTB functions. The protein exists in oligomeric as well as monomeric form. The central part of PTB (amino acids 169-293) plays a major role in the oligomerization. PTB contains several RNA-binding motifs. Among them, the C-terminal part of PTB (amino acids 329-530) exhibited the strongest RNA-binding activity. The N-terminal part of PTB is responsible for the enhancement of RNA binding by HeLa cell cytoplasmic factor(s).

摘要

多嘧啶序列结合蛋白(PTB)参与前体mRNA剪接和内部核糖体进入位点依赖性翻译。为了理解PTB功能的分子基础,对PTB不同片段的生化特性进行了分析。该蛋白以寡聚体和单体形式存在。PTB的中央部分(氨基酸169 - 293)在寡聚化中起主要作用。PTB包含多个RNA结合基序。其中,PTB的C末端部分(氨基酸329 - 530)表现出最强的RNA结合活性。PTB的N末端部分负责HeLa细胞质因子增强RNA结合。

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