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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family.
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Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family.

机译：真核硒蛋白的多样性和功能可塑性：SelJ家族的鉴定和表征。

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摘要

Selenoproteins are a diverse group of proteins that contain selenocysteine (Sec), the 21st amino acid. In the genetic code, UGA serves as a termination signal and a Sec codon. This dual role has precluded the automatic annotation of selenoproteins. Recent advances in the computational identification of selenoprotein genes have provided a first glimpse of the size, functions, and phylogenetic diversity of eukaryotic selenoproteomes. Here, we describe the identification of a selenoprotein family named SelJ. In contrast to known selenoproteins, SelJ appears to be restricted to actinopterygian fishes and sea urchin, with Cys homologues only found in cnidarians. SelJ shows significant similarity to the jellyfish J1-crystallins and with them constitutes a distinct subfamily within the large family of ADP-ribosylation enzymes. Consistent with its potential role as a structural crystallin, SelJ has preferential and homogeneous expression in the eye lens in early stages of zebrafish development. A structural role for SelJ would be in contrast to the majority of known selenoenzymes. The unusually highly restricted phylogenetic distribution of SelJ, its specialization, and the comparative analysis of eukaryotic selenoproteomes reveal the diversity and functional plasticity of selenoproteins and point to a mosaic evolution of the use of Sec in proteins.
机译：硒蛋白是包含硒代半胱氨酸（Sec）（第21个氨基酸）的多种蛋白质。在遗传密码中，UGA充当终止信号和Sec密码子。这种双重作用排除了硒蛋白的自动注释。硒蛋白基因的计算鉴定的最新进展提供了真核硒蛋白组的大小，功能和系统发育多样性的第一印象。在这里，我们描述了一个名为SelJ的硒蛋白家族的鉴定。与已知的硒蛋白相反，SelJ似乎仅限于放线翅目鱼类和海胆，而Cys同源物仅在虫中发现。 SelJ显示出与水母J1-crystallins的显着相似性，并且与它们构成了ADP-核糖基化酶大家族中的一个独特的亚家族。与它作为结构性晶状蛋白的潜在作用相一致，SelJ在斑马鱼发育的早期阶段在眼晶状体内具有优先且均匀的表达。 SelJ的结构性作用与大多数已知的硒酶相反。 SelJ的异常严重的系统发育分布，其专业化以及对真核硒蛋白组的比较分析揭示了硒蛋白的多样性和功能可塑性，并指出了在蛋白质中使用Sec的镶嵌进化。

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