ArticleThe Journal of biological chemistry2015
Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 65 citations in OpenAlex.
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- A disease-causing isoleucyl-tRNA synthetase variant leads to altered protein complex formation and cellular stress response.The Journal of biological chemistry · 2026Article
- AIMP3 maintains cardiac homeostasis by regulating the editing activity of methionyl-tRNA synthetase.Nature cardiovascular research · 2025Article
- EPRS1-mediated fibroblast activation and mitochondrial dysfunction promote kidney fibrosis.Experimental & molecular medicine · 2024Article
- Phosphocode-dependent glutamyl-prolyl-tRNA synthetase 1 signaling in immunity, metabolism, and disease.Experimental & molecular medicine · 2023Review
- Solution X-ray scattering highlights discrepancies in Plasmodium multi-aminoacyl-tRNA synthetase complexes.Protein science : a publication of the Protein Society · 2023Article
- RNA granule-clustered mitochondrial aminoacyl-tRNA synthetases form multiple complexes with the potential to fine-tune tRNA aminoacylation.Nucleic acids research · 2022Article
- Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1.Nature communications · 2022Article
- Glutamyl-prolyl-tRNA synthetase 1 coordinates early endosomal anti-inflammatory AKT signaling.Nature communications · 2022Article
- Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein.The Journal of biological chemistry · 2022Article
- AIMP2-DX2 provides therapeutic interface to control KRAS-driven tumorigenesis.Nature communications · 2022Article
- Review
- Structure and Dynamics of the Human Multi-tRNA Synthetase Complex.Sub-cellular biochemistry · 2022Article
- Disease-associated mutations in a bifunctional aminoacyl-tRNA synthetase gene elicit the integrated stress response.The Journal of biological chemistry · 2021Article
- Structural basis for the dynamics of human methionyl-tRNA synthetase in multi-tRNA synthetase complexes.Nucleic acids research · 2021Article
- Tryptophanyl-tRNA Synthetase as a Potential Therapeutic Target.International journal of molecular sciences · 2021Review
- The zinc-binding domain of mammalian prolyl-tRNA synthetase is indispensable for catalytic activity and organism viability.iScience · 2021Article
- Article
- 3-Dimensional architecture of the human multi-tRNA synthetase complex.Nucleic acids research · 2020Article
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Authors and funding
14 authors at 8 institutions in 3 countries.
Funding
Abstract
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 MSC components, 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 GST-containing cellular factors.
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