Nikonova E Yu, Mihaylina A O, Lekontseva N V, Nikonov O S, Klyashtorny V G, Kravchenko O V, Andreev D E, Shatsky I N, Garber M B
Biofizika. 2016 Mar-Apr;61(2):277-85.
Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charge a tRNA molecule with a cognate amino acid required for protein synthesis. Glycyl-tRNA synthetase is one of the most interesting aminoacyl-tRNA synthetases due to its structure variability and functional features in the different organisms. It was shown recently that human glycyl-tRNA synthetase is a regulator of translational initiation of poliovirus mRNA. Details of this process and its mechanism still remain unknown. While exploring this stage of poliovirus functioning we have studied the interaction of the cytoplasmic form of human glycyl-tRNA synthetase and its domains with the fragments of the poliovirus IRES element. As a result, we have identified the minimal fragment of viral mRNA with which glycyl-tRNA synthetase fully interacts and estimated the contribution of some domains to the interaction of glycyl-tRNA synthetase with RNA.
氨酰-tRNA合成酶是一个古老的酶家族，它能将蛋白质合成所需的同源氨基酸特异性地加载到tRNA分子上。甘氨酰-tRNA合成酶是最有趣的氨酰-tRNA合成酶之一，因为它在不同生物体中的结构变异性和功能特性。最近有研究表明，人甘氨酰-tRNA合成酶是脊髓灰质炎病毒mRNA翻译起始的调节因子。这一过程及其机制的细节仍然未知。在探索脊髓灰质炎病毒功能的这一阶段时，我们研究了人甘氨酰-tRNA合成酶的细胞质形式及其结构域与脊髓灰质炎病毒内部核糖体进入位点（IRES）元件片段的相互作用。结果，我们确定了与甘氨酰-tRNA合成酶完全相互作用的病毒mRNA最小片段，并评估了一些结构域对甘氨酰-tRNA合成酶与RNA相互作用的贡献。
