{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["111(42)"],"submitter":["Fu Y"],"pubmed_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"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["15084-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4210331"],"repository":["biostudies-literature"],"pubmed_title":["Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation."],"pmcid":["PMC4210331"],"pubmed_authors":["Jeon YH","Kim D","Cho Y","Jo CH","Wang D","Park M","Fu Y","Kim HS","Kim S","Jin KS","Kim MH","Kim Y","Kim JH","Kwon NH","Hwang KY"],"additional_accession":[]},"is_claimable":false,"name":"Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.","description":"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","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Oct","modification":"2026-05-04T11:47:18.601Z","creation":"2025-05-31T22:57:54.661Z"},"accession":"S-EPMC4210331","cross_references":{"pubmed":["25288775"],"doi":["10.1073/pnas.1408836111"]}}