Indel-driven evolution of the canavanine tRNA-editing deacetylase enzyme CtdA.

ABSTRACT: Proteins are heteropolymers composed of twenty standard amino acids, but over 500 non-proteogenic amino acids exist in nature that can be misincorporated into proteins. Canavanine is an antimetabolite of the chemically similar L-arginine. It can be utilized by bacteria such as Pseudomonas canavaninivorans in the legume rhizome as a sole source of carbon and nitrogen. However, canavanine misincorporates in proteins of this bacterium as its arginyl-tRNA synthetase loads tRNA^Arg with both canavanine and arginine. Canavanyl-tRNA^Arg deacetylase (CtdA) removes canavanine from misloaded tRNA^Arg, preventing its protein toxicity, being the first enzyme known to edit tRNA mischarged with a non-proteinogenic amino acid. We have elucidated CtdA's crystal structu

SUBMITTER: Tabagari N 

PROVIDER: S-EPMC12268091 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature