anticodon and alpha-aminobutyric-acid

Accuracy in protein biosynthesis is maintained through multiple pathways, with a critical checkpoint occurring at the tRNA aminoacylation step catalyzed by aminoacyl-tRNA synthetases (ARSs). In addition to the editing functions inherent to some synthetases, single-domain trans-editing factors, which are structurally homologous to ARS editing domains, have evolved as alternative mechanisms to correct mistakes in aminoacyl-tRNA synthesis. To date, ARS-like trans-editing domains have been shown to act on specific tRNAs that are mischarged with genetically encoded amino acids. However, structurally related non-protein amino acids are ubiquitous in cells and threaten the proteome. Here, we show that a previously uncharacterized homolog of the bacterial prolyl-tRNA synthetase (ProRS) editing domain edits a known ProRS aminoacylation error, Ala-tRNA

Topics: Alanine; Amino Acyl-tRNA Synthetases; Aminobutyrates; Anticodon; Binding Sites; Codon; Escherichia coli; Kinetics; Molecular Docking Simulation; Mutation; Nucleic Acid Conformation; Proline; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Rhodopseudomonas; RNA Processing, Post-Transcriptional; RNA, Transfer, Pro; Substrate Specificity; Transfer RNA Aminoacylation