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Glycyl-tRNA synthetase

W Freist1, D T Logan, D H Gauss

  • 1Max-Planck-Institut für experimentelle Medizin, Göttingen, Germany.

Biological Chemistry Hoppe-Seyler
|June 1, 1996
PubMed
Summary

Glycyl-tRNA synthetase (GlyRS) is crucial for protein synthesis and may regulate cell functions. Its diverse structures and primordial features suggest an ancient role in evolution, with implications for diseases like polymyositis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Glycyl-tRNA synthetase (GlyRS) is a class II aminoacyl-tRNA synthetase essential for incorporating glycine into proteins.
  • GlyRS also synthesizes dinucleoside polyphosphates, potentially regulating cellular functions.
  • Glycine, the simplest amino acid, has an ancient evolutionary origin as a protein component.

Purpose of the Study:

  • To explore the structural diversity and evolutionary significance of Glycyl-tRNA synthetase.
  • To understand the mechanism of glycyl-tRNA synthesis and enzyme-substrate recognition.
  • To investigate the potential link between GlyRS and autoimmune diseases.

Main Methods:

  • Sequence analysis of nine GlyRS genes from six organisms.
  • Determination of the crystal structure of the alpha 2 GlyRS from Thermus thermophilus.
  • Analysis of antibody presence in patient sera.

Main Results:

  • GlyRS exhibits diverse oligomeric structures (alpha 2 beta 2 and alpha 2) across organisms.
  • The alpha 2 enzyme structure reveals three domains: active site, anticodon recognition, and acceptor stem interaction.
  • Antibodies against GlyRS are found in patients with polymyositis and interstitial lung disease.

Conclusions:

  • GlyRS possesses characteristics of a primordial enzyme, with conserved recognition elements for tRNAGly.
  • The enzyme's structural plasticity and dual function suggest a complex role in cellular processes.
  • The presence of anti-GlyRS antibodies indicates a potential role in autoimmune pathogenesis.

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