Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0081734
Title: Reinvestigation of aminoacyl-TRNA synthetase core complex by affinity purification-mass spectrometry reveals TARSL2 as a potential member of the complex
Authors: Kim, K.
Park, S.-J.
Na, S.
Kim, J.S.
Choi, H. 
Kim, Y.K.
Paek, E.
Lee, C.
Issue Date: 2-Dec-2013
Citation: Kim, K., Park, S.-J., Na, S., Kim, J.S., Choi, H., Kim, Y.K., Paek, E., Lee, C. (2013-12-02). Reinvestigation of aminoacyl-TRNA synthetase core complex by affinity purification-mass spectrometry reveals TARSL2 as a potential member of the complex. PLoS ONE 8 (12) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0081734
Abstract: 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. © 2013 Kim et al.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/108793
ISSN: 19326203
DOI: 10.1371/journal.pone.0081734
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