Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
- Authors
- Fu, Yaoyao; Kim, Youngran; Jin, Kyeong Sik; Kim, Hyun Sook; Kim, Jong Hyun; Wang, DongMing; Park, Minyoung; Jo, Chang Hwa; Kwon, Nam Hoon; Kim, Doyeun; Kim, Myung Hee; Jeon, Young Ho; Hwang, Kwang Yeon; Kim, Sunghoon; Cho, Yunje
- Issue Date
- 21-10월-2014
- Publisher
- NATL ACAD SCIENCES
- Keywords
- arginyl-tRNA synthetase; multisynthetase complex; crystal structure; AIMP1; glutaminyl-tRNA synthetase
- Citation
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.111, no.42, pp.15084 - 15089
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Volume
- 111
- Number
- 42
- Start Page
- 15084
- End Page
- 15089
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/97074
- DOI
- 10.1073/pnas.1408836111
- ISSN
- 0027-8424
- 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.
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Collections - College of Pharmacy > Department of Pharmaceutical Science > 1. Journal Articles
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