2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 52(2018) N 1 p. 7-14; DOI 10.1134/S0026893318010156 Full Text

E.Yu. Nikonova*, A.O. Mihaylina, M.S. Nemchinova, M.B. Garber, O.S. Nikonov

Glycyl-tRNA Synthetase as a Potential Universal Regulator of Translation Initiation at IRES-I

Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia

Received - 2017-04-06; Accepted - 2017-05-18

A full analysis has been conducted of the sequences and secondary structures of viral type-I or related IRESs identified in all of the elements that correspond to the previously described minimal fragment of the enterovirus C IRES, which mimics the glycine tRNA anticodon hairpin in the IRES structure and is necessary for the specific binding of glycyl-tRNA synthetase. Experiments on human glycyl-tRNA synthetase binding with the mRNA fragments of several taxonomically distant viruses showed that the binding constants of these complexes are similar. These results indicate that the regulation of translation initiation via glycyl-tRNA synthetase must be a universal mechanism for these viruses and the corresponding parts of their mRNAs must have similar spatial structures. Furthermore, at least one additional mRNA hairpin with the glycyl anticodon loop has been found in all analyzed viral type-I IRESs. It seems plausible that this extra hairpin is associated with the second RNA-binding site of the glycyl-tRNA synthetase dimer and stabilizes its complex with the viral mRNA.

Glycyl-tRNA synthetase, picornaviruses, enteroviruses, poliovirus, translational initiation, IRES, IRES I