Kim, Kyutae Park, Seong-Jun Na, Seungjin Kim, Jun Seok Choi, Hyungwon Kim, Yoon Ki Paek, Eunok Lee, Cheolju 2024-01-20T11:01:21Z 2024-01-20T11:01:21Z 2021-09-05 2013-12-02 1932-6203 https://pubs.kist.re.kr/handle/201004/127345 Twenty different aminoacyl-tRNA synthetases (ARSs) link each amino acid to their cognate tRNAs. Individual ARSs are also associated with various non-canonical activities involved in neuronal diseases, cancer and autoimmune diseases. Among them, eight ARSs (D, EP, I, K, L, M, Q and RARS), together with three ARS-interacting multifunctional proteins (AIMPs), are currently known to assemble the multi-synthetase complex (MSC). However, the cellular function and global topology of MSC remain unclear. In order to understand the complex interaction within MSC, we conducted affinity purification-mass spectrometry (AP-MS) using each of AIMP1, AIMP2 and KARS as a bait protein. Mass spectrometric data were funneled into SAINT software to distinguish true interactions from background contaminants. A total of 40, 134, 101 proteins in each bait scored over 0.9 of SAINT probability in HEK 293T cells. Complex-forming ARSs, such as DARS, EPRS, IARS, Kars, LARS, MARS, QARS and RARS, were constantly found to interact with each bait. Variants such as, AIMP2-DX2 and AIMP1 isoform 2 were found with specific peptides in KARS precipitates. Relative enrichment analysis of the mass spectrometric data demonstrated that TARSL2 (threonyl-tRNA synthetase like-2) was highly enriched with the ARS-core complex. The interaction was further confirmed by coimmunoprecipitation of TARSL2 with other ARS core-complex components. We suggest TARSL2 as a new component of ARS core-complex. English PUBLIC LIBRARY SCIENCE PROTEIN INTERACTIONS BREAST-CANCER C-MYC TRANSLATION ASSIGNMENT INTERACTS TARGET SIGNAL FANCD2 AIMP2 Reinvestigation of Aminoacyl-TRNA Synthetase Core Complex by Affinity Purification-Mass Spectrometry Reveals TARSL2 as a Potential Member of the Complex Article 10.1371/journal.pone.0081734 1 PLOS ONE, v.8, no.12 PLOS ONE 8 12 scie scopus 000327944500092 2-s2.0-84891622583 Multidisciplinary Sciences Science & Technology - Other Topics Article PROTEIN INTERACTIONS BREAST-CANCER C-MYC TRANSLATION ASSIGNMENT INTERACTS TARGET SIGNAL FANCD2 AIMP2