Determination of the minimal fragment of the poliovirus IRES that is necessary for the formation of a specific complex with the human glycyl-tRNA synthetase
Autor: | M. B. Garber, E. Yu. Nikonova, O. S. Nikonov, Dmitry E. Andreev, Ivan N. Shatsky, V. G. Klyashtorny, O. V. Kravchenko, A. O. Mihaylina, N. V. Lekontseva |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
chemistry.chemical_classification Messenger RNA 030102 biochemistry & molecular biology Poliovirus Biophysics RNA Biology medicine.disease_cause Amino acid 03 medical and health sciences Internal ribosome entry site Biochemistry chemistry Cytoplasm RNA-Protein Interaction medicine Protein biosynthesis |
Zdroj: | Biophysics. 61:233-240 |
ISSN: | 1555-6654 0006-3509 |
Popis: | Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charge a tRNA molecule with a cognate amino acid that is required for protein synthesis. Glycyl-tRNA synthetase is one of the most interesting aminoacyl-tRNA synthetases due to its structural variability and functional features in different organisms. Recently, it has been shown that human glycyl-tRNA synthetase is a regulator of translational initiation of poliovirus mRNA. The details and mechanisms of this process are still unknown. While exploring the stage of poliovirus functioning, we studied the interactions of the cytoplasmic form of human glycyl-tRNA synthetase and its domains with fragments of the poliovirus IRES element. As a result, we identified the minimal fragment of the viral mRNA that glycyl-tRNA synthetase adequately interacts with and we estimated the contribution of some of the domains to the interaction between glycyl-tRNA synthetase and RNA. |
Databáze: | OpenAIRE |
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