期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 42, 页码 15084-15089出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1408836111
关键词
arginyl-tRNA synthetase; multisynthetase complex; crystal structure; AIMP1; glutaminyl-tRNA synthetase
资金
- National R&D Program for Cancer Control, Ministry for Health and Welfare [1020280]
- National Research Foundation of Korea Grant [1020280]
- Ministry of Education, Science, and Technology (MEST) Grants [2012004028, 2012-054226, 20120008833]
- Rising Star Program of the Pohang University of Science and Technology
- Brain Korea 21 Program of the Korean Ministry of Education
- MEST Grant [2013044795]
- Korea Health Promotion Institute [1020280] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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