Available online at www.sciencedirect.com ScienceDirect Indirect tRNA aminoacylation during accurate translation and phenotypic mistranslation 1 1 Udumbara M Rathnayake , Whitney N Wood and Tamara L Hendrickson The fact that most bacteria do not contain a full set of In fact, the glutaminyl-tRNA and/or asparaginyl-tRNA aminoacyl-tRNA synthetases (aaRS) is often synthetases (GlnRS and AsnRS, respectively) are missing underappreciated. In the absence of asparaginyl-tRNA and/or from most microorganisms. In the absence of one or both Asn glutaminyl-tRNA synthetase (AsnRS and GlnRS), Asn-tRNA of these enzymes, an indirect path to aminoacylate the Gln and/or Gln-tRNA are produced by an indirect tRNA corresponding tRNAs (Figure 1) replaces the canonical aminoacylation pathway that relies on misacylation of these direct aminoacylation routes . This two-step process two tRNAs by two different misacylating aaRSs, followed by utilizes a non-discriminating aspartyl-tRNA synthetase transamidation by an amidotransferase (GatCAB in bacteria). (ND-AspRS) [5 ] and a misacylating glutamyl-tRNA This review highlights the central importance of indirect tRNA synthetase (either ND-GluRS  or GluRS2 [7,8 ], see Asn Gln aminoacylation to accurate protein translation, mechanistic below for details) to misacylate tRNA and tRNA , peculiarities that appear to be unique to this system, and the respectively. In bacteria, the
Current Opinion in Chemical Biology – Elsevier
Published: Dec 1, 2017
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