Aminoacyl-tRNA synthetase complexes in evolution

Area of Science:

• Biochemistry
• Molecular Biology
• Cell Biology

Background:

• Aminoacyl-tRNA synthetases (aaRS) are vital enzymes that translate the genetic code by linking specific amino acids to their corresponding tRNA molecules.
• Beyond their canonical role in translation, aaRS participate in diverse non-translational cellular pathways crucial for homeostasis.
• In eukaryotes, aaRS often assemble into large multi-aminoacyl-tRNA synthetase complexes (MARS), influencing their functional states.

Purpose of the Study:

• To review the composition and assembly of MARS complexes across various organisms, from archaea to mammals.
• To elucidate the significance of MARS in organizing the translation apparatus.
• To explore the dual roles of aaRS, encompassing both translational and non-translational functions, particularly in relation to MARS.

Main Methods:

• Literature review of studies on MARS composition and function.
• Comparative analysis of MARS assembly across different taxa.
• Synthesis of current knowledge on the interplay between MARS association and cellular homeostasis.

Main Results:

• Diverse MARS compositions exist across archaea, eukaryotes, and mammals.
• MARS assembly is a conserved feature, suggesting a key organizational role in the translation machinery.
• Dynamic association and dissociation of aaRS within MARS complexes allow for switching between translational and non-translational functions.

Conclusions:

• MARS complexes are fundamental for eukaryotic translation and cellular regulation.
• The assembly and disassembly of MARS provide a mechanism for modulating aaRS activity and function.
• Understanding MARS is critical for comprehending cellular homeostasis and the broader roles of aaRS.