CONSERVED NUCLEOTIDE-SEQUENCES IN THE OPEN READING FRAME AND 3' UNTRANSLATED REGION OF SELENOPROTEIN-P MESSENGER-RNA
CONSERVED NUCLEOTIDE-SEQUENCES IN THE OPEN READING FRAME AND 3' UNTRANSLATED REGION OF SELENOPROTEIN-P MESSENGER-RNA
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DOI：
10.1073/pnas.90.2.537
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发表时间：
1993-01-15
影响因子：
11.1
通讯作者：
BURK, RF
中科院分区：
文献类型：
--
作者：
HILL, KE;LLOYD, RS;BURK, RF
大鼠肝脏硒蛋白P的一级结构中含有10个硒半胱氨酸残基(推测)。它是迄今为止唯一一种具有多个硒半胱氨酸残基的硒蛋白。从人肝脏和心脏的cDNA文库中克隆了硒蛋白P的基因，并对其进行了序列测定。开放阅读框是相同的，并包含一个信号肽，这表明蛋白质是由两个器官分泌的，因此并不是只在肝脏产生。有10个硒半胱氨酸残基(推定)。比较人和大鼠的开放阅读框，发现核苷酸序列的同源性为69%，推导的氨基酸序列的同源性为72%。3‘端非编码区的两个区域在人和大鼠之间具有高度的保守性。这些区域中的每一个都包含一个预测的稳定的茎环结构，类似于在I型碘甲状腺原氨酸、5‘-脱碘酶和谷胱甘肽过氧化物酶的3’非翻译区中报道的单个茎环结构。I型碘甲状腺原氨酸5‘-脱碘酶的茎环结构已被证明是在UGA密码子上掺入硒半胱氨酸残基所必需的。由于在硒蛋白P mRNA的3‘非翻译区只存在两个茎环结构，因此可以得出结论，每个硒半胱氨酸残基不需要单独的茎环结构。
Rat liver selenoprotein P contains 10 selenocysteine residues in its primary structure (deduced). It is the only selenoprotein characterized to date that has more than one selenocysteine residue. Selenoprotein P cDNA has been cloned from human liver and heart cDNA libraries and sequenced. The open reading frames are identical and contain a signal peptide, indicating that the protein is secreted by both organs and is therefore not exclusively produced in the liver. Ten selenocysteine residues (deduced) are present. Comparison of the open reading frame of the human cDNA with the rat cDNA reveals a 69% identity of the nucleotide sequence and 72% identity of the deduced amino acid sequence. Two regions in the 3' untranslated portion have high conservation between human and rat. Each of these regions contains a predicted stable stem-loop structure similar to the single stem-loop structures reported in 3' untranslated regions of type I iodothyronine 5'-deiodinase and glutathione peroxidase. The stem-loop structure of type I iodothyronine 5'-deiodinase has been shown to be necessary for incorporation of the selenocysteine residue at the UGA codon. Because only two stem-loop structures are present in the 3' untranslated region of selenoprotein P mRNA, it can be concluded that a separate stem-loop structure is not required for each selenocysteine residue.