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J Biol Chem, Vol. 274, Issue 24, 16673-16676, June 11, 1999

COMMUNICATION
Precursor of Pro-apoptotic Cytokine Modulates Aminoacylation Activity of tRNA Synthetase

Sang Gyu Park, Keum Hee Jung, Jong Sang Lee, Yeong Joon Jo, Hiromi Motegi^§, Sunghoon Kim, and Kiyotaka Shiba^§

From the  National Creative Research Initiatives Center for ARS Network, Sung Kyun Kwan University, Suwon, Kyunggido, 440-746, Korea and the ^§ Department of Cell Biology, Cancer Institute, Japanese Foundation for Cancer Research, Tokyo 170-8455, Japan

Endothelial monocyte activating polypeptide II (EMAPII) is a cytokine that is specifically induced by apoptosis. Its precursor (pro-EMAPII) has been suggested to be identical to p43, which is associated with the multi-tRNA synthetase complex. Herein, we have demonstrated that the N-terminal domain of pro-EMAPII interacts with the N-terminal extension of human cytoplasmic arginyl-tRNA synthetase (RRS) using genetic and immunoprecipitation analyses. Aminoacylation activity of RRS was enhanced about 2.5-fold by the interaction with pro-EMAPII but not with its N- or C-terminal domains alone. The N-terminal extension of RRS was not required for enzyme activity but did mediate activity stimulation by pro-EMAPII. Pro-EMAPII reduced the apparent K_m of RRS to tRNA, whereas the k_cat value remained unchanged. Therefore, the precursor of EMAPII is a multi-functional protein that assists aminoacylation in normal cells and releases the functional cytokine upon apoptosis.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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