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Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability

Academic Article
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Overview

authors

  • Beebe, K.
  • Ribas de Pouplana, L.
  • Schimmel, Paul

publication date

  • February 2003

journal

  • EMBO Journal  Journal

abstract

  • Editing of misactivated amino acids by class I tRNA synthetases is encoded by a specialized internal domain specific to class I enzymes. In contrast, little is known about editing activities of the structurally distinct class II enzymes. Here we show that the class II alanyl-tRNA synthetase (AlaRS) has a specialized internal domain that appears weakly related to an appended domain of threonyl-tRNA synthetase (ThrRS), but is unrelated to that found in class I enzymes. Editing of misactivated glycine or serine was shown to require a tRNA cofactor. Specific mutations in the aforementioned domain disrupt editing and lead to production of mischarged tRNA. This class-specific editing domain was found to be essential for cell growth, in the presence of elevated concentrations of glycine or serine. In contrast to ThrRS, where the editing domain is not found in all three kingdoms of living organisms, it was incorporated early into AlaRSs and is present throughout evolution. Thus, tRNA-dependent editing by AlaRS may have been critical for making the genetic code sufficiently accurate to generate the tree of life.

subject areas

  • Adenosine Triphosphate
  • Alanine-tRNA Ligase
  • Amino Acid Sequence
  • Animals
  • Cell Survival
  • Evolution, Molecular
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Phenotype
  • Phylogeny
  • Point Mutation
  • Protein Structure, Tertiary
  • RNA Editing
  • RNA, Transfer
  • Sequence Alignment
  • Threonine-tRNA Ligase
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Research

keywords

  • editing domain
  • evolution of genetic code
  • genetic code
  • tRNA cofactor
  • tRNA mischarging
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Identity

PubMed Central ID

  • PMC140749

International Standard Serial Number (ISSN)

  • 0261-4189

Digital Object Identifier (DOI)

  • 10.1093/emboj/cdg065

PubMed ID

  • 12554667
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Additional Document Info

start page

  • 668

end page

  • 675

volume

  • 22

issue

  • 3

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