Determination of the Minimal Fragment of the Poliovirus IRES Necessary for the Formation of a Specific Complex with the Human Glycyl-tRNA Synthetase

• Published in: Biofizika Vol. 61; no. 2; p. 277
• Main Authors: 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
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-03-2016
• Subjects: Amino Acids - chemistry; Cytoplasm - chemistry; Glycine-tRNA Ligase - chemistry; Glycine-tRNA Ligase - genetics; Humans; Poliovirus - chemistry; Poliovirus - enzymology; Protein Biosynthesis; RNA, Messenger - chemistry; RNA, Messenger - genetics; RNA, Transfer - chemistry; RNA, Transfer - genetics
• ISSN: 0006-3029

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.