Abstract

The macromolecular tRNA synthetase complex consists of nine different enzymes and three non-enzymatic factors. This complex was recently shown to be a novel signalosome, since many of its components are involved in signaling pathways in addition to their catalytic roles in protein synthesis. The structural organization and dynamic relationships of the components of the complex are not well understood. Here we performed a systematic depletion analysis to determine the effects of structural intimacy and the turnover of the components. The results showed that the stability of some components depended on their neighbors. Lysyl-tRNA synthetase was most independent of other components for its stability whereas it was most required for the stability of other components. Arginyl- and methionyl-tRNA synthetases had the opposite characteristics. Thus, the systematic depletion of the components revealed the functional reason for the complex formation and the assembly pattern of these multi-functional enzymes and their associated factors.

Highlights

  • Since many cellular proteins exert their biological effects via the formation of macromolecular complexes, it is important to understand the pattern of assembly and dynamic relationships of the components of such complexes

  • Aminoacyl-tRNA synthetases (ARSs)3 are essential enzymes catalyzing the ligation of their cognate amino acids and tRNAs in the process of translation

  • Molecular Assembly of Aminoacyl-tRNA Synthetase Complex nique and determined how this affected the stability of the other components, as well as protein synthesis

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Summary

Introduction

The systematic depletion of the components revealed the functional reason for the complex formation and the assembly pattern of these multi-functional enzymes and their associated factors. Since many cellular proteins exert their biological effects via the formation of macromolecular complexes, it is important to understand the pattern of assembly and dynamic relationships of the components of such complexes.

Results
Conclusion
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