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首页> 外文期刊>Journal of cellular biochemistry. >Recognition and binding of the human selenocysteine insertion sequence by nucleolin.
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Recognition and binding of the human selenocysteine insertion sequence by nucleolin.

机译：核仁素对人硒代半胱氨酸插入序列的识别和结合。

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摘要

Prokaryotic and eukaryotic cells cotranslationally incorporate the unusual amino acid selenocysteine at a UGA codon, which conventionally serves as a termination signal. Translation of selenoprotein gene transcripts in eukaryotes depends upon a "selenocysteine insertion sequence" in the 3'-untranslated region. We have previously shown that DNA-binding protein B specifically binds this sequence element. We now report the identification of nucleolin as a partner in the selenoprotein translation complex. In RNA electromobility shift assays, nucleolin binds the selenocysteine insertion sequence from the human cellular glutathione peroxidase gene, competes with binding activity from COS cells, and shows diminished affinity for probes with mutations in functionally important, conserved sequence elements. Antibody to nucleolin interferes with the gel shift activity of COS cell extract. Antibody to DNA-binding protein B co-extracts nucleolin from HeLa cell cytosol, and the two proteins co-sediment in glycerol gradient fractions of ribosomal high salt extracts. Thus, nucleolin appears to join DNA-binding protein B and possibly other partners to form a large complex that links the selenocysteine insertion sequence in the 3'-untranslated region to other elements in the coding region and ribosome to translate the UGA "stop" codon as selenocysteine. Copyright 2000 Wiley-Liss, Inc.
机译：原核和真核细胞在UGA密码子上共翻译并包含异常氨基酸硒代半胱氨酸，通常用作终止信号。真核生物中硒蛋白基因转录物的翻译取决于3'非翻译区中的“硒代半胱氨酸插入序列”。先前我们已经表明，DNA结合蛋白B特异性结合此序列元素。我们现在报告鉴定为硒蛋白翻译复合物中的伴侣的核仁素。在RNA电动迁移分析中，核仁素与人细胞谷胱甘肽过氧化物酶基因的硒代半胱氨酸插入序列结合，与COS细胞的结合活性竞争，并且对功能上重要的保守序列元件中具有突变的探针的亲和力降低。核仁蛋白抗体会干扰COS细胞提取物的凝胶迁移活性。 DNA结合蛋白B的抗体从HeLa细胞胞质溶胶中共提取核仁蛋白，而这两种蛋白在核糖体高盐提取物的甘油梯度级分中共同沉淀。因此，核仁蛋白似乎会结合DNA结合蛋白B和可能的其他伴侣，形成一个大型复合物，该复合物将3'-非翻译区的硒代半胱氨酸插入序列与编码区和核糖体中的其他元件连接起来，从而翻译UGA“终止”密码子如硒代半胱氨酸。版权所有2000 Wiley-Liss，Inc.

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