Assembly of multi-tRNA synthetase complex via heterotetrameric glutathione transferase-homology domains

Ha Yeon Cho, Seo Jin Maeng, Hyo Je Cho, Yoon Seo Choi, Jeong Min Chung, Sangmin Lee, Hoi Kyoung Kim, Jong Hyun Kim, Chi Yong Eom, Yeon Gil Kim, Min Guo, Hyun Suk Jung, Beom Sik Kang, Sunghoon Kim

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54 Citations (Scopus)


Many multicomponent protein complexes mediating diverse cellular processes are assembled through scaffolds with specialized protein interaction modules. The multi-tRNA synthetase complex (MSC), consisting of nine different aminoacyl-tRNA synthetases and three non-enzymatic factors (AIMP1-3), serves as a hub for many signaling pathways in addition to its role in protein synthesis. However, the assembly process and structural arrangement of the MSC components are not well understood. Here we show the heterotetrameric complex structure of the glutathione transferase (GST) domains shared among the four MSCcomponents, methionyl-tRNA synthetase (MRS), glutaminyl-prolyl-tRNA synthetase (EPRS), AIMP2 and AIMP3. The MRS-AIMP3 and EPRS-AIMP2 using interface 1 are bridged via interface 2 of AIMP3 and EPRS to generate a unique linear complex of MRS-AIMP3:EPRS-AIMP2 at the molar ratio of (1:1):(1: 1). Interestingly, the affinity at interface 2 of AIMP3:EPRS can be varied depending on the occupancy of interface 1, suggesting the dynamic nature of the linear GST tetramer. The four components are optimally arranged for maximal accommodation of additional domains and proteins. These characteristics suggest the GST tetramer as a unique and dynamic structural platform from which the MSC components are assembled. Considering prevalence of the GST-like domains, this tetramer can also provide a tool for the communication of the MSC with other GSTcontaining cellular factors.

Original languageEnglish
Pages (from-to)29313-29328
Number of pages16
JournalJournal of Biological Chemistry
Issue number49
Publication statusPublished - 2015 Dec 4

Bibliographical note

Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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