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Updated: Jun 24, 2026

Conjugative Mating Assays for Sequence-specific Analysis of Transfer Proteins Involved in Bacterial Conjugation
Published on: January 4, 2017
[tRNA-dependent editing of errors by prolyl-tRNA synthetase from bacteria Enterococcus faecalis]
Abstract:
Maintenance of amino acid specificity by aminoacyl-tRNA synthetases, particularly prolyl-tRNA synthetase, requires for not only specific recognition of homologic amino acid, but also missynthesized products hydrolysis, known as editing. The speeding-up of the enzymatic hydrolysis of missynthesized alanyl adenylate by bacteria Enterococcus faecalis prolyl-tRNA synthetase in the presence of tRNAPro, and also importance for this function of 2'- and 3'-hydroxyle groups of tRNA 3'-terminal adenosine ribose is shown in the work. Furthermore, results are shown, that support the absence of editing (INS) domain role in alanyl adenylate hydrolysis. Possible significance of tRNA-dependent alanyl adenylate hydrolysis by prolyl-tRNA synthetase for prolyl-tRNAPro synthesis specificity maintenance is discussed.
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