Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
SCIE
SCOPUS
- Title
- Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
- Authors
- Fu, YY; Kim, Y; Jin, KS; Kim, HS; Kim, JH; Wang, D; Park, M; Jo, CH; Kwon, NH; Kim, D; Kim, MH; Jeon, YH; Hwang, KY; Kim, S; CHO, YUNJE
- Date Issued
- 2014-10-21
- Publisher
- National Academy of Sciences
- Abstract
- In higher eukaryotes, one of the two arginyl-tRNA synthetases (ArgRSs) has evolved to have an extended N-terminal domain that plays a crucial role in protein synthesis and cell growth and in integration into the multisynthetase complex (MSC). Here, we report a crystal structure of the MSC subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43. In this complex, the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. Mutation of AIMP1 destabilized the N-terminal helix of ArgRS and abrogated its catalytic activity. Mutation of the N-terminal helix of ArgRS liberated GlnRS, which is known to control cell death. This ternary complex was further anchored to AIMP2/p38 through interaction with AIMP1. These findings demonstrate the importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/12774
- DOI
- 10.1073/PNAS.1408836111
- ISSN
- 0027-8424
- Article Type
- Article
- Citation
- Proceedings of the National Academy of Sciences of the United States of America, vol. 111, no. 42, page. 15084 - 15089, 2014-10-21
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