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A more recent version of this article appeared on December 15, 2006
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M605211200v1
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Papers In Press, published online ahead of print October 24, 2006
J. Biol. Chem, 10.1074/jbc.M605211200
Submitted on May 31, 2006
Revised on October 23, 2006
Accepted on October 24, 2006

Hierarchical network between the components of the multi-tRNA synthetase complex: Implications for complex formation

Jung Min Han, Min Ji Lee, Sang Gyu Park, Sun Hee Lee, Ehud Razin, Eung-Chil Choi, and Sunghoon Kim

College of Pharmacy, Center for ARS Network, Seoul 151-742

Corresponding Author: sungkim{at}snu.ac.kr

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.


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