Expanding a tyrosyl-tRNA synthetase assay to other aminoacyl-tRNA synthetases

Aminoacyl-tRNA synthetases catalyze the attachment of amino acids to their cognate tRNAs, in general, aminoacyl-tRNA synthetase assays require stoichiometric amounts of tRNA, which limits their sensitivity while increasing their cost. This requirement for stoichiometric amounts of tRNA can be alleviated if the aminoacyl-tRNA product is cleaved following the tRNA aminoacylation reaction, regenerating the free tRNA substrate. This data article is related to the research article entitled "A continuous tyrosyl-tRNA synthetase assay that regenerates the tRNA substrate" in which this approach is used to develop a continuous spectrophotometric assay for tyrosyl-tRNA synthetase [1]. Here we present enzymes that can be used to cleave the aminoacyltRNA product for at least 16 of the 20 naturally occurring amino acids. These enzymes can be used to extend the tyrosyl-tRNA synthetase assay to other aminoacyl-tRNA synthetases. (C) 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license.