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首页> 外文期刊>Molecular and Cellular Biology >The Redox State of SECIS Binding Protein 2 Controls Its Localization and Selenocysteine Incorporation Function
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The Redox State of SECIS Binding Protein 2 Controls Its Localization and Selenocysteine Incorporation Function

机译：SECIS结合蛋白2的氧化还原状态控制其定位和硒代半胱氨酸掺入功能。

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摘要

Selenoproteins are central controllers of cellular redox homeostasis. Incorporation of selenocysteine (Sec) into selenoproteins employs a unique mechanism to decode the UGA stop codon. The process requires the Sec insertion sequence (SECIS) element, tRNASec, and protein factors including the SECIS binding protein 2 (SBP2). Here, we report the characterization of motifs within SBP2 that regulate its subcellular localization and function. We show that SBP2 shuttles between the nucleus and the cytoplasm via intrinsic, functional nuclear localization signal and nuclear export signal motifs and that its nuclear export is dependent on the CRM1 pathway. Oxidative stress induces nuclear accumulation of SBP2 via oxidation of cysteine residues within a redox-sensitive cysteine-rich domain. These modifications are efficiently reversed in vitro by human thioredoxin and glutaredoxin, suggesting that these antioxidant systems might regulate redox status of SBP2 in vivo. Depletion of SBP2 in cell lines using small interfering RNA results in a decrease in Sec incorporation, providing direct evidence for its requirement for selenoprotein synthesis. Furthermore, Sec incorporation is reduced substantially after treatment of cells with agents that cause oxidative stress, suggesting that nuclear sequestration of SBP2 under such conditions may represent a mechanism to regulate the expression of selenoproteins.
机译：硒蛋白是细胞氧化还原稳态的主要控制者。将硒代半胱氨酸（Sec）掺入硒蛋白中采用了独特的机制来解码UGA终止密码子。该过程需要Sec插入序列（SECIS）元素，tRNA Sec 和包括SECIS结合蛋白2（SBP2）在内的蛋白质因子。在这里，我们报告调节其亚细胞定位和功能的SBP2内的图案的表征。我们显示SBP2穿梭之间通过固有的，功能性的核定位信号和核出口信号图案的核和细胞质之间，其核出口取决于CRM1途径。氧化应激通过氧化还原敏感的富含半胱氨酸的域内的半胱氨酸残基的氧化诱导SBP2的核积累。这些修饰在体外可被人硫氧还蛋白和谷氨酸还原酶有效地逆转，表明这些抗氧化剂系统可能在体内调节SBP2的氧化还原状态。使用小的干扰RNA在细胞系中消耗SBP2会导致Sec掺入的减少，从而为其所需的硒蛋白合成提供了直接证据。此外，用引起氧化应激的试剂处理细胞后，Sec的掺入量显着降低，这表明在这种条件下SBP2的核螯合可能代表了一种调节硒蛋白表达的机制。

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