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Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.

Siqi Wu1, Li Zheng1,2, Zhoufei Hei1

  • 1State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences, 345 Lingling Road, Shanghai, 200032, China.

Cellular and Molecular Life Sciences : CMLS
|February 8, 2022
PubMed
Summary

The multi-tRNA synthetase complex (MSC) likely evolved in animals to shield aminoacyl-tRNA synthetases, like human lysyl-tRNA synthetase (LysRS), from cellular pathway interference and maintain protein translation fidelity.

Keywords:
aminoacyl-tRNA synthetase complex-interacting multifunctional proteinlysyl-tRNA synthetasemulti aminoacyl-tRNA synthetase complexnoncanonical functionprotein translational machinery

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Aminoacyl-tRNA synthetases (aaRSs) are essential for protein synthesis.
  • The multi-tRNA synthetase complex (MSC) is conserved in eukaryotes but its evolutionary origin is unclear.
  • Human lysyl-tRNA synthetase (LysRS) is a component of the MSC and has moonlighting functions.

Purpose of the Study:

  • To investigate the structural dynamics and functional role of human LysRS in relation to the MSC.
  • To understand the evolutionary advantage of MSC formation in metazoans.
  • To elucidate the protective role of MSC scaffold proteins on aaRS activity.

Main Methods:

  • Crystallography
  • CRISPR/Cas9-based genome editing
  • Biochemistry
  • Cell biology analyses

Main Results:

  • Metazoan LysRS structures exhibit greater dynamism than those from unicellular organisms.
  • The scaffold protein AIMP2 stabilizes human LysRS in a closed conformation, preserving aminoacylation activity under stress.
  • AIMP2 deletion in HEK293 cells impairs cell growth in nutrient-deficient conditions.
  • Free human LysRS can be modified or recruited for non-canonical functions.

Conclusions:

  • The MSC likely evolved in metazoans to protect aaRS components from non-canonical functions and maintain essential aminoacylation activity.
  • AIMP2 plays a crucial role in stabilizing LysRS and ensuring cellular function under stress.
  • MSC formation represents an evolutionary adaptation for maintaining protein synthesis fidelity in multicellular organisms.