Abstract
A major element ensuring the accuracy of translation of the genetic code is the recognition of tRNA by its cognate aminoacyl-tRNA synthetase. The tRNA molecule assumes many of the unusual elements of RNA structure (Delarue and Moras, 1989), and presumably this flexibility and variety in structure leads to the role of tRNA in other metabolic functions additional to protein synthesis (Sö11, 1993). The application of a variety of genetic, biochemical and biophysical techniques have been used to elucidate factors determining the accuracy of the recognition by Escherichia coli glutaminyl-tRNA synthetase (G1nRS) for tRNAG1n, and this system is probably one of the best understood tRNA:aminoacyl-tRNA synthetase systems (Söll, 1990), resulting in the first RNA-protein structure determined at the molecular level (Rould et al., 1989; Rould et al., 1991). This review will focus on our current understanding of this RNA:protein interaction.
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Rogers, M.J. et al. (1993). Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA. In: Nierhaus, K.H., Franceschi, F., Subramanian, A.R., Erdmann, V.A., Wittmann-Liebold, B. (eds) The Translational Apparatus. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2407-6_5
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