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J Biol Chem, Vol. 273, Issue 18, 11267-11273, May 1, 1998

A Multifunctional Repeated Motif Is Present in Human Bifunctional tRNA Synthetase

Seung Bae RhoDagger , Jong Sang LeeDagger , Eui-Jun Jeong§, Key-Sun Kim§, Yang Gyun Kim, and Sunghoon KimDagger

From the Dagger  Department of Biology, Sung Kyun Kwan University, 300 Chunchundong, Jangangu, Suwon, Kyunggido 440-746, Korea, the § Structural Biology Center, Korea Institute of Science and Technology, Cheongryang Box 131, Seoul 136-791, Korea, and the  Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Tandem repeats located in the human bifunctional glutamyl-prolyl-tRNA synthetase (EPRS) have been found in many different eukaryotic tRNA synthetases and were previously shown to interact with another distinct repeated motifs in human isoleucyl-tRNA synthetase. Nuclear magnetic resonance and differential scanning calorimetry analyses of an isolated EPRS repeat showed that it consists of a helix-turn-helix with a melting temperature of 59 °C. Specific interaction of the EPRS repeats with those of isoleucyl-tRNA synthetase was confirmed by in vitro binding assays and shown to have a dissociation constant of approximately 2.9 µM. The EPRS repeats also showed the binding activity to the N-terminal motif of arginyl-tRNA synthetase as well as to various nucleic acids, including tRNA. Results of the present work suggest that the region comprising the repeated motifs of EPRS provides potential sites for interactions with various biological molecules and thus plays diverse roles in the cell.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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