Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains | |
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 |
2015-12-04 | |
卷号 | 290期号:49页码:29313-29328 |
ISSN号 | 0021-9258 |
DOI | 10.1074/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. |
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关键词 | PROTEIN-PROTEIN INTERACTIONS ; 3-DIMENSIONAL STRUCTURE ; STRUCTURE REFINEMENT ; DENSITY MODIFICATION ; CRYSTAL-STRUCTURE ; TRANSLATION ; REVEALS ; SOFTWARE ; PARTICLE ; BINDING |
WOS研究方向 | Biochemistry & Molecular Biology |
语种 | 英语 |
出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
WOS记录号 | WOS:000366613400019 |
内容类型 | 期刊论文 |
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. |
个性服务 |
查看访问统计 |
相关权益政策 |
暂无数据 |
收藏/分享 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论