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Structural Aspects of Phenylalanylation and Quality Control in Three Major Forms of Phenylalanyl-tRNA Synthetase

机译:苯丙氨酰-tRNA合成酶的三种主要形式的苯丙氨酰化和质量控制的结构方面

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摘要

Aminoacyl-tRNA synthetases (aaRSs) are a canonical set of enzymes that specifically attach corresponding amino acids to their cognate transfer RNAs in the cytoplasm, mitochondria, and nucleus. The aaRSs display great differences in primary sequence, subunit size, and quaternary structure. Existence of three types of phenylalanyl-tRNA synthetase (PheRS)—bacterial (αβ)2, eukaryotic/archaeal cytosolic (αβ)2, and mitochondrial α—is a prominent example of structural diversity within the aaRSs family. Although archaeal/eukaryotic and bacterial PheRSs share common topology of the core domains and the B3/B4 interface, where editing activity of heterotetrameric PheRSs is localized, the detailed investigation of the three-dimensional structures from three kingdoms revealed significant variations in the local design of their synthetic and editing sites. Moreover, as might be expected from structural data eubacterial, Thermus thermophilus and human cytoplasmic PheRSs acquire different patterns of tRNAPhe anticodon recognition.
机译:氨酰基-tRNA合成酶(aaRSs)是一组典型的酶,可将相应的氨基酸特异地连接到其在​​细胞质,线粒体和细胞核中的同源转移RNA。 aaRS在一级序列,亚基大小和四级结构上显示出很大的差异。三种类型的苯丙氨酰-tRNA合成酶(PheRS)的存在-细菌(αβ)2,真核/古细菌胞质(αβ)2和线粒体α-是aaRSs家族内结构多样性的一个突出例子。尽管古细菌/真核生物和细菌PheRS共享核心结构域和B3 / B4接口的共同拓扑,异四聚体PheRS的编辑活性位于该结构中,但是对三个王国的三维结构的详细研究显示,在本地设计中存在显着差异。他们的合成和编辑网站。此外,正如真细菌的结构数据所预期的那样,嗜热栖热菌和人类细胞质PheRSs获得不同的tRNAPhe反密码子识别模式。

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