Molecular cloning, characterization and mRNA expression analysis of a novel selenoprotein: avian selenoprotein W from chicken
Molecular cloning, characterization and mRNA expression analysis of a novel selenoprotein: avian selenoprotein W from chicken
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DOI：
10.1007/s11033-010-0520-5
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发表时间：
2011-08-01
影响因子：
2.8
通讯作者：
Tang, Zhao-Xin
中科院分区：
文献类型：
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作者：
Li, Jin-Long;Ruan, Hong-Feng;Tang, Zhao-Xin
本研究从鸡脑组织中克隆了一种新的禽硒蛋白W （SelW）基因。该基因的完整核苷酸序列包含一个258 bp的开放阅读框，编码85个氨基酸。生物信息学方法鉴定出鸡SelW蛋白具有β - α - β - β - α二级结构模式，其中β(1)和β(2)是平行链，形成经典的β (1)- α (1)- β(2)基序，这也在硫氧还蛋白样折叠蛋白中观察到。该蛋白具有一个候选CXXU氧化还原基序，位于β(1)和α(1)之间的环（残基10-13）。小鼠和鸡的SelW蛋白在三维结构上的相似性表明它们可能具有相似的功能。此外，SelW mRNA的3'-非翻译区发现了硒代半胱氨酸插入序列（SECIS）元件。SECIS元素被归类为形式II。此外，我们分析了SelW基因在36只60日龄鸡不同组织中的mRNA表达；SelW在所有组织中均有表达，表明SelW在鸡组织中广泛表达。因此，我们认为SelW可能在鸟类硒的生化功能中起重要作用。
In this study, a novel avian selenoprotein W (SelW) gene was cloned from chicken cerebral tissue. The complete nucleotide sequence of the gene contained a 258 bp open reading frame encoding 85 amino acids. Bioinformatics approaches identified the chicken SelW protein is characterized by a beta-alpha-beta-beta-beta-alpha secondary structure pattern, wherein beta(1) and beta(2) are parallel strands forming a classical beta(1)-alpha(1)-beta(2) motif, which is also observed in thioredoxin-like fold proteins. The protein has a candidate CXXU redox motif which is located in the loop (residues 10-13) between beta(1) and alpha(1). The 3D structural similarity between mouse and chicken SelW protein suggests that the proteins may exhibit similar functions. Additionally, a selenocysteine insertion sequence (SECIS) element was found in the 3'-untranslated region of the SelW mRNA. The SECIS element was classified as form II. Moreover, we analyzed the mRNA expression of SelW genes in 36 different tissues of 60-day-old chickens; the expression of SelW was detected in all tissues, indicating that SelW is expressed widely in chicken tissue. Hence, we suggest that SelW might play an important role in the biochemical functions of Se in birds.