Aminoacyl-tRNA synthetases and the evolution of coded peptide synthesis: The Thioester World

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Abstract

Coded peptide synthesis must have been preceded by a prebiotic stage, in which thioesters played key roles. Fossils of the Thioester World are found in extant aminoacyl-tRNA synthetases (AARSs). Indeed, studies of the editing function reveal that AARSs have a thiol-binding site in their catalytic modules. The thiol-binding site confers the ability to catalyze aminoacyl~coenzyme A thioester synthesis and peptide bond formation. Genomic comparisons show that AARSs are structurally related to proteins involved in sulfur and coenzyme A metabolisms and peptide bond synthesis. These findings point to the origin of the amino acid activation and peptide bond synthesis functions in the Thioester World and suggest that the present-day AARSs had originated from ancestral forms that were involved in noncoded thioester-dependent peptide synthesis.

Original languageEnglish (US)
Pages (from-to)469-481
Number of pages13
JournalFEBS Letters
Volume590
Issue number4
DOIs
StatePublished - Feb 1 2016

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Keywords

  • aminoacyl-tRNA synthetase
  • coenzyme A
  • evolution
  • homocysteine editing
  • noncoded peptide synthesis
  • prebiotic chemistry

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