Abstract
Glutamyl-tRNA synthetases (GluRSs) are divided into two distinct types, with regard to the presence or absence of glutaminyl-tRNA synthetase (GlnRS) in the genetic translation systems. In the original 19-synthetase systems lacking GlnRS, the 'non-discriminating' GluRS glutamylates both tRNAGlu and tRNAGln. In contrast, in the evolved 20-synthetase systems with GlnRS, the 'discriminating' GluRS aminoacylates only tRNAGlu. Here we report the 2.4 Å resolution crystal structure of a 'discriminating' GluRS·tRNAGlu complex from Thermus thermophilus. The GluRS recognizes the tRNAGlu anticodon bases via two α-helical domains, maintaining the base stacking. We show that the discrimination between the Glu and Gln anticodons (34YUC36 and 34YUG36, respectively) is achieved by a single arginine residue (Arg 358). The mutation of Arg 358 to Gln resulted in a GluRS that does not discriminate between the Glu and Gln anticodons. This change mimics the reverse course of GluRS evolution from anticodon 'non-dicsriminating' to 'discriminating'.
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Acknowledgements
S.Y. is the recipient of Grants-in-Aid for Science Research on Priority Areas from the Ministry of Education, Science, Sports and Culture of Japan; S.S. was supported by grants from the JSPS Research Fellowships for Young Scientists and from the RIKEN Special Postdoctoral Researchers Program.
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Sekine, Si., Nureki, O., Shimada, A. et al. Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase. Nat Struct Mol Biol 8, 203–206 (2001). https://doi.org/10.1038/84927
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DOI: https://doi.org/10.1038/84927
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