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首页> 外文期刊>The protein journal >Critical role of zinc ion on E. coli glutamyl-queuosine-tRNAAsp synthetase (Glu-Q-RS) structure and function
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Critical role of zinc ion on E. coli glutamyl-queuosine-tRNAAsp synthetase (Glu-Q-RS) structure and function

机译：锌离子对大肠杆菌谷氨酰奎宁-tRNAAsp合成酶（Glu-Q-RS）的结构和功能的关键作用

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摘要

Glutamyl-queuosine-tRNAAsp synthetase (Glu-Q-RS) and glutamyl-tRNA synthetase (GluRS), differ widely by their function although they share close structural resemblance within their catalytic core of GluRS. In particular both Escherichia coli GluRS and Glu-Q-RS contain a single zinc-binding site in their putative tRNA acceptor stem-binding domain. It has been shown that the zinc is crucial for correct positioning of the tRNA Glu acceptor-end in the active site of E. coli GluRS. To address the role of zinc ion inGlu-Q-RS, the C101S/C103S Glu-Q-RS variant is constructed. Energy dispersive X-ray fluorescence show that the zinc ion still remained coordinated but the variant became structurally labile and acquired aggregation capacity. The extent of aggregation of the protein is significantly decreased in presence of the small substrates and more particularly by adenosine triphosphate. Addition of zinc increased significantly the solubility of the variant. The aminoacylation assay reveals a decrease in activity of the variant even after addition of zinc as compared to the wild-type, although the secondary structure of the protein is not altered as shown by the Fourier transform infrared spectroscopy study.
机译：谷氨酰-奎宁-tRNAAsp合成酶（Glu-Q-RS）和谷氨酰-tRNA合成酶（GluRS），尽管它们在GluRS的催化核心内具有相似的结构相似性，但它们的功能差异很大。特别地，大肠杆菌GluRS和Glu-Q-RS在其推定的tRNA受体茎结合域中均​​含有单个锌结合位点。已经显示锌对于在大肠杆菌GluRS的活性位点中正确定位tRNA Glu受体端至关重要。为了解决锌离子在Glu-Q-RS中的作用，构建了C101S / C103S Glu-Q-RS变体。能量色散X射线荧光显示锌离子仍保持配位，但变体在结构上不稳定并获得聚集能力。在存在小的底物的情况下，尤其是通过三磷酸腺苷，蛋白质的聚集程度显着降低。锌的添加显着增加了变体的溶解度。尽管如傅立叶变换红外光谱研究所示，蛋白质的二级结构没有改变，但是与野生型相比，即使在添加锌后，氨酰化测定仍显示变体活性降低。

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