Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation

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Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation
Y Fu; Y Kim; K S Jin; H S Kim; J H Kim; D M Wang; M Park; C H Jo; N H Kwon; D Kim; Myung Hee Kim; Y H Jeon; K Y Hwang; S Kim; Y Cho
Bibliographic Citation
Proceedings of National Academy of Sciences of United States of America, vol. 111, no. 42, pp. 15084-15089
Publication Year
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.
AIMP1Arginyl-tRNA synthetaseCrystal structureGlutaminyl-tRNA synthetaseMultisynthetase complex
Natl Acad Sciences
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Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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