A standalone editing protein deacylates mischarged canavanyl-tRNAArg to prevent canavanine incorporation into proteins

Franziskus Hauth, Dietmar Funck, Jörg S Hartig

Nucleic Acids Research, gkac1197, https://doi.org/10.1093/nar/gkac1197

Error-free translation is one of the most vital processes in all living organisms, but can be substantially challenged by compounds that mimic amino acids. Canavanine, or 5-oxa-arginine, is used as an antimetabolite by higher plants that is toxic due to its incorporation into proteins. We report the discovery of a standalone editing protein specifically deacylating canavanylated tRNAArg that enables the legume rhizosphere inhabitant Pseudomonas canavaninivorans to prevent canavanine mis-incorporation into its proteome. Our results are the first to show editing activity towards mischarged tRNAArg and add to the puzzle of how faithful translation is ensured in nature.

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