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The evolution of Class II Aminoacyl-tRNA synthetases and the first code.

Temple F Smith1, Hyman Hartman2

  • 1BioMedical Engineering, Boston University, Boston, MA 02215, USA.

FEBS Letters
|October 17, 2015
PubMed
Summary

Class II Aminoacyl-tRNA synthetases evolved from a three-peptidyl-hairpin core. Their ancient origins and split into two divisions suggest a transition from a thioester to a phosphate ester world before the genetic code existed.

Keywords:
Aminoacyl-tRNA-synthetaseEvolutionOperational-codeThioester

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Area of Science:

  • Biochemistry
  • Molecular Evolution
  • Origin of Life Studies

Background:

  • Class II Aminoacyl-tRNA synthetases are ancient, multi-domain proteins crucial for protein synthesis.
  • Their catalytic domain's evolution is traceable to a primordial three-peptidyl-hairpin structure.

Purpose of the Study:

  • To reconstruct the evolutionary pathway of the Class II Aminoacyl-tRNA synthetase catalytic domain.
  • To investigate the paradox of synthetase structure predating the genetic code.
  • To propose a model for the early evolution of aminoacyl-tRNA synthetases.

Main Methods:

  • Phylogenetic analysis of Class II synthetase domains.
  • Comparative analysis of protein structures and sequences.
  • Hypothetical reconstruction of ancestral protein structures.

Main Results:

  • The catalytic domain evolved from a three-peptidyl-hairpin core.
  • Early evolution led to a split into two divisions, possibly linked to the operational code.
  • The earliest operational code likely encoded Glycine, Proline, Alanine, and Lysine/Aspartic acid.

Conclusions:

  • Aminoacyl-tRNA synthetase evolution predates the genetic code, presenting a paradox.
  • This paradox can be resolved by proposing their formation during a transition from a thioester to a phosphate ester world.