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Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains

文献类型：期刊论文

作者Cho, Ha Yeon2; Maeng, Seo Jin2; Cho, Hyo Je2; Choi, Yoon Seo2; Chung, Jeong Min3; Lee, Sangmin3; Kim, Hoi Kyoung4; Kim, Jong Hyun4; Eom, Chi-Yong5; Kim, Yeon-Gil6
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
出版日期2015-12-04
卷号290期号:49页码:29313-29328
ISSN号0021-9258
DOI10.1074/jbc.M115.690867
文献子类Article
英文摘要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 GST-containing cellular factors.
WOS关键词PROTEIN-PROTEIN INTERACTIONS ; 3-DIMENSIONAL STRUCTURE ; STRUCTURE REFINEMENT ; DENSITY MODIFICATION ; CRYSTAL-STRUCTURE ; TRANSLATION ; REVEALS ; SOFTWARE ; PARTICLE ; BINDING
资助项目Global Frontier Project Grant of the National Research Foundation - Ministry of Science, ICT & Future Planning (MSIP) of Korea[NRF-2014M3A6A4062857]
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:000366613400019
出版者AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
源URL[http://119.78.100.183/handle/2S10ELR8/276286]  
专题中国科学院上海药物研究所
通讯作者Kang, Beom Sik
作者单位1.Shanghai Inst Mat Med, Natl Ctr Drug Screening, Shanghai 201203, Peoples R China
2.Kyungpook Natl Univ, Sch Life Sci & Biotechnol, KNU Creat BioRes Grp, Taegu 702701, South Korea;
3.Kangwon Natl Univ, Coll Nat Sci, Dept Biochem, Chunchon 200701, South Korea;
4.Seoul Natl Univ, Grad Sch Convergence Technol, Med Bioconvergence Res Ctr, Dept Mol Med & Biopharmaceut Sci, Seoul 151742, South Korea;
5.Korea Basic Sci Inst, Western Seoul Ctr, NanoBio Convergence Res Team, Seoul 120750, South Korea;
6.Pohang Univ Sci & Technol, Pohang Accelerator Lab, Pohang 790834, South Korea;
7.Scripps Res Inst, Dept Canc Biol, Jupiter, FL 33458 USA;
推荐引用方式
GB/T 7714		 Cho, Ha Yeon,Maeng, Seo Jin,Cho, Hyo Je,et al. Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2015,290(49):29313-29328.
APA Cho, Ha Yeon.,Maeng, Seo Jin.,Cho, Hyo Je.,Choi, Yoon Seo.,Chung, Jeong Min.,...&Kim, Sunghoon.(2015).Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.JOURNAL OF BIOLOGICAL CHEMISTRY,290(49),29313-29328.
MLA Cho, Ha Yeon,et al."Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains".JOURNAL OF BIOLOGICAL CHEMISTRY 290.49(2015):29313-29328.

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来源：上海药物研究所

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