Anticodon recognition in evolution: switching tRNA specificity of an aminoacyl-tRNA synthetase by site-directed peptide transplantation

The Journal of Biological Chemistry
Annie BrevetP Plateau

Abstract

The highly conserved aspartyl-, asparaginyl-, and lysyl-tRNA synthetases compose one subclass of aminoacyl-tRNA synthetases, called IIb. The three enzymes possess an OB-folded extension at their N terminus. The function of this extension is to specifically recognize the anticodon triplet of the tRNA. Three-dimensional models of bacterial aspartyl- and lysyl-tRNA synthetases complexed to tRNA indicate that a rigid scaffold of amino acid residues along the five beta-strands of the OB-fold accommodates the base U at the center of the anticodon. The binding of the adjacent anticodon bases occurs through interactions with a flexible loop joining strands 4 and 5 (L45). As a result, a switching of the specificity of lysyl-tRNA synthetase from tRNALys (anticodon UUU) toward tRNAAsp (GUC) could be attempted by transplanting the small loop L45 of aspartyl-tRNA synthetase inside lysyl-tRNA synthetase. Upon this transplantation, lysyl-tRNA synthetase loses its capacity to aminoacylate tRNALys. In exchange, the chimeric enzyme acquires the capacity to charge tRNAAsp with lysine. Upon giving the tRNAAsp substrate the discriminator base of tRNALys, the specificity shift is improved. The change of specificity was also established in vivo. Inde...Continue Reading

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Citations

Jun 24, 2010·Nucleic Acids Research·Randall A Hughes, Andrew D Ellington
Mar 1, 2005·FEBS Letters·Su-Ni Tang, Jing-Fei Huang
Dec 21, 2004·Biochemical and Biophysical Research Communications·Benjamin S Szwergold, Sundeep Lal
Oct 29, 2009·Journal of Computational Chemistry·Anne LopesThomas Simonson
Dec 18, 2015·Proteins·Thomas SimonsonPierre Plateau
Oct 19, 2012·Biochemistry·John J Perona, Andrew Hadd

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