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分子克隆、鉴定及新型硒蛋白基因 mRNA 表达分析:鸡的硒蛋白 W。

Molecular cloning, characterization and mRNA expression analysis of a novel selenoprotein: avian selenoprotein W from chicken.

机构信息

College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.

出版信息

Mol Biol Rep. 2011 Aug;38(6):4015-22. doi: 10.1007/s11033-010-0520-5. Epub 2010 Dec 4.

Abstract

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 β-α-β-β-β-α secondary structure pattern, wherein β1 and β2 are parallel strands forming a classical β1-α1-β2 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 β1 and α1. 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.

摘要

在这项研究中,从鸡脑组织中克隆了一种新型的禽类硒蛋白 W (SelW)基因。该基因的完整核苷酸序列包含一个 258bp 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 蛋白的特征是具有 β-α-β-β-β-α 二级结构模式,其中 β1 和 β2 是形成经典的 β1-α1-β2 基序的平行链,该基序也存在于硫氧还蛋白样折叠蛋白中。该蛋白具有一个候选的 CXXU 氧化还原模体,位于 β1 和 α1 之间的环(残基 10-13)中。鼠和鸡 SelW 蛋白的 3D 结构相似性表明,这些蛋白可能具有相似的功能。此外,在 SelW mRNA 的 3'非翻译区发现了一个硒代半胱氨酸插入序列 (SECIS) 元件。该 SECIS 元件被归类为 II 型。此外,我们分析了 60 日龄鸡 36 种不同组织中 SelW 基因的 mRNA 表达;在所有组织中都检测到 SelW 的表达,表明 SelW 在鸡组织中广泛表达。因此,我们认为 SelW 可能在鸟类 Se 的生化功能中发挥重要作用。

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