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Updated: Aug 21, 2026

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
Published on: August 1, 2016
Aminoacylation of the anticodon stem by a tRNA-synthetase paralog: relic of an ancient code?
Henri Grosjean1, Valérie de Crécy-Lagard, Glenn R Björk
1Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, F-91198 Gif-sur-Yvette, France. Grosjean@lebs.cnrs-gif.fr
Abstract:
The activation and charging of amino acids onto the acceptor stems of their cognate tRNAs are the housekeeping functions of aminoacyl-tRNA synthetases. The availability of whole genome sequences has revealed the existence of synthetase-like proteins that have other functions linked to different aspects of cell metabolism and physiology. In eubacteria, a paralog of glutamyl-tRNA synthetase, which lacks the tRNA-binding domain, was found to aminoacylate tRNA(Asp) not on the 3'-hydroxyl group of the acceptor stem but on a cyclopentene diol of the modified nucleoside queuosine present at the wobble position of anticodon loop. This modified nucleoside might be a relic of an ancient code.
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