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Updated: Jun 18, 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
Deciphering synonymous codons in the three domains of life: co-evolution with specific tRNA modification enzymes
Henri Grosjean1, Valérie de Crécy-Lagard, Christian Marck
1Université Paris-Sud, CNRS, UMR8621, Institut de Génétique et de Microbiologie, Orsay F-91405, France. henri.grosjean@igmors.u-psud.fr
Abstract:
The strategies organisms use to decode synonymous codons in cytosolic protein synthesis are not uniform. The complete isoacceptor tRNA repertoire and the type of modified nucleoside found at the wobble position 34 of their anticodons were analyzed in all kingdoms of life. This led to the identification of four main decoding strategies that are diversely used in Bacteria, Archaea and Eukarya. Many of the modern tRNA modification enzymes acting at position 34 of tRNAs are present only in specific domains and obviously have arisen late during evolution. In an evolutionary fine-tuning process, these enzymes must have played an essential role in the progressive introduction of new amino acids, and in the refinement and standardization of the canonical nuclear genetic code observed in all extant organisms (functional convergent evolutionary hypothesis).
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