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Identification of the residues involved in the unique serine specificity of Caenorhabditis elegans mitochondrial EF-Tu2

机译：鉴定参与Caenorhabdise秀丽隐患Mitochondrial EF-Tu2的独特丝氨酸特异性的残留物

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摘要

In canonical translation systems, the single elongation factor Tu (EF-Tu) recognizes all elongator tRNAs. However, in Caenorhabditis elegans mitochondria, two distinct EF-Tu species, EF-Tu1 and EF-Tu2, recognize 20 species of T armless tRNA and two species of D armless tRNA(Ser), respectively. We previously reported that C. elegans mitochondrial EF-Tu2 specifically recognizes the serine moiety of serylated-tRNA. In this study, to identify the critical residues for the serine specificity in EF-Tu2, several residues in the amino acid binding pocket of bacterial EF-Tu were systematically replaced with corresponding EF-Tu2 residues, and the mutants were analyzed for their specificity for esterified amino acids attached to tRNAs. In this way, we obtained a bacterial EF-Tu mutant that acquired serine specificity after the introduction of 10 EF-Tu2 residues into its amino acid binding pocket. C. elegans EF-Tu2 mutants lacking serine specificity were also created by replacing seven or eight residues with bacterial residues. Further stressing the importance of these residues, we found that they are almost conserved in EF-Tu2 sequences of closely related nematodes. Thus, these three approaches reveal the critical residues essential for the unique serine specificity of C. elegans mitochondrial EF-Tu2.
机译：在规范翻译系统中，单伸长率因子Tu（EF-TU）识别所有细长TrNA。然而，在Caenorhabditis elegans线粒体中，两个不同的EF-TU物种，EF-TU1和EF-TU2，识别20种T的无臂TRNA和两种D Imbless TRNA（SER）。我们之前报道了C. Elegans线粒体EF-Tu2具体识别酶化-TRNA的丝氨酸部分。在该研究中，为了鉴定EF-TU2中的丝氨酸特异性的关键残留物，用相应的EF-TU2残基系统地替换细菌EF-Tu的氨基酸结合口袋中的几个残基，并分析突变体的特异性酯化氨基酸附着在TrNAs上。以这种方式，我们获得了一种细菌EF-Tu突变体，其在将10个EF-TU2残基引入其氨基酸结合口袋后获得丝氨酸特异性。 C.秀丽隐杆线虫EF-TU2缺乏丝氨酸特异性的突变体也通过用细菌残留物替换七或八个残留物而产生。进一步强调这些残留物的重要性，我们发现它们几乎保守在密切相关的线虫的EF-Tu2序列中。因此，这三种方法揭示了对秀丽隐杆线虫线粒体EF2的独特丝氨酸特异性所必需的临界残留物。

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