Indirect tRNA aminoacylation during accurate translation and phenotypic mistranslation

Indirect tRNA aminoacylation during accurate translation and phenotypic mistranslation 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 [3]. 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 [6] 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Chemical Biology Elsevier

Indirect tRNA aminoacylation during accurate translation and phenotypic mistranslation

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier Ltd
ISSN
1367-5931
D.O.I.
10.1016/j.cbpa.2017.10.009
Publisher site
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Abstract

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 [3]. 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 [6] 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

Journal

Current Opinion in Chemical BiologyElsevier

Published: Dec 1, 2017

References

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