biostudies-literatureUnknown111(42)Fu YIn 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. MutationProceedings of the National Academy of Sciences of the United States of America15084-9https://www.ebi.ac.uk/biostudies/studies/S-EPMC4210331biostudies-literatureStructure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.PMC4210331Jeon YHKim DCho YJo CHWang DPark MFu YKim HSKim SJin KSKim MHKim YKim JHKwon NHHwang KYfalseStructure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.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. Mutation2014-01-01T00:00:00Z2014 Oct2026-05-04T11:47:18.601Z2025-05-31T22:57:54.661ZS-EPMC42103312528877510.1073/pnas.1408836111