Feb 3, 2016

Aminoacyl-tRNA Synthetases and the Evolution of Coded Peptide Synthesis: The Thioester World

FEBS Letters
H Jakubowski


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 non-coded thioester-dependent peptide synthesis. This article is protected by copyright. All rights reserved.

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Mentioned in this Paper

Chemical Bond
Thioester Biosynthetic Process
Activation of Amino Acids
Coenzyme A Metabolic Process
Peptide Biosynthesis
Coenzyme A
MT-TA gene

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