Previously it was shown that the primary binding site of human glycyl-tRNA synthetase on IRES type I is formed by an apical part of its fifth domain and the anticodon binding domain of human glycyl-tRNA synthetase is responsible for specificity of interactions. In this paper, we have shown that glycyl-tRNA synthetase is able to interact with the other stem-loop regions of the IRES type I located outside the fifth domain. These fragments, like the previously determined once, mimic the anticodon hairpin of glycine tRNA and contain the glycine anticodon in the loop also. Apparently, the anticodon-binding domain of glycyl-tRNA synthetase is also responsible for specific interactions with these parts of the viral mRNA. The obtained data confirm our suggestion on the existence of an additional binding site for the homodimer of human glycyl-tRNA synthetase on IRES type I.
viruses, enterovirus, translation initiation, human glycyl-tRNA synthetase, IRES, RNA-protein interaction
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