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J. Biol. Chem., Vol. 281, Issue 50, 38663-38667, December 15, 2006

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Hierarchical Network between the Components of the Multi-tRNA Synthetase Complex

IMPLICATIONS FOR COMPLEX FORMATION^*

Jung Min Han¹, Min Ji Lee¹, Sang Gyu Park, Sun Hee Lee, Ehud Razin^¶, Eung-Chil Choi, and Sunghoon Kim²

From the Imagene Company Biotechnology Incubating Center, Golden Helix, Seoul National University, Seoul 151-741, Korea, the National Creative Research Initiatives Center for ARS Network, College of Pharmacy, Seoul National University, Seoul 151-741, Korea, and the ^¶Department of Biochemistry, Hebrew University Hadassah Medical School, Jerusalem 91120, Israel

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.

Received for publication, May 31, 2006 , and in revised form, October 23, 2006.

^* This work was supported by a grant from National Creative Research Initiatives of the Ministry of Science and Technology, Korea and a grant from the Korea-Israel Scientific Research Cooperation of KOSEF. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Methods and supplemental Figs. 1-4 and Table 1.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 82-2-880-8180; Fax: 82-2-875-2621; E-mail: sungkim{at}snu.ac.kr.

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