Reinvestigation of Aminoacyl-TRNA Synthetase Core Complex by Affinity Purification-Mass Spectrometry Reveals TARSL2 as a Potential Member of the Complex
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Kyutae | - |
dc.contributor.author | Park, Seong-Jun | - |
dc.contributor.author | Na, Seungjin | - |
dc.contributor.author | Kim, Jun Seok | - |
dc.contributor.author | Choi, Hyungwon | - |
dc.contributor.author | Kim, Yoon Ki | - |
dc.contributor.author | Paek, Eunok | - |
dc.contributor.author | Lee, Cheolju | - |
dc.date.accessioned | 2022-07-16T07:08:32Z | - |
dc.date.available | 2022-07-16T07:08:32Z | - |
dc.date.created | 2021-05-12 | - |
dc.date.issued | 2013-12 | - |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/161327 | - |
dc.description.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. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | PUBLIC LIBRARY SCIENCE | - |
dc.title | Reinvestigation of Aminoacyl-TRNA Synthetase Core Complex by Affinity Purification-Mass Spectrometry Reveals TARSL2 as a Potential Member of the Complex | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Paek, Eunok | - |
dc.identifier.doi | 10.1371/journal.pone.0081734 | - |
dc.identifier.scopusid | 2-s2.0-84891622583 | - |
dc.identifier.wosid | 000327944500092 | - |
dc.identifier.bibliographicCitation | PLOS ONE, v.8, no.12, pp.1 - 14 | - |
dc.relation.isPartOf | PLOS ONE | - |
dc.citation.title | PLOS ONE | - |
dc.citation.volume | 8 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 1 | - |
dc.citation.endPage | 14 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | PROTEIN INTERACTIONS | - |
dc.subject.keywordPlus | BREAST-CANCER | - |
dc.subject.keywordPlus | C-MYC | - |
dc.subject.keywordPlus | TRANSLATION | - |
dc.subject.keywordPlus | ASSIGNMENT | - |
dc.subject.keywordPlus | INTERACTS | - |
dc.subject.keywordPlus | TARGET | - |
dc.subject.keywordPlus | SIGNAL | - |
dc.subject.keywordPlus | FANCD2 | - |
dc.subject.keywordPlus | AIMP2 | - |
dc.identifier.url | https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0081734 | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
222, Wangsimni-ro, Seongdong-gu, Seoul, 04763, Korea+82-2-2220-1365
COPYRIGHT © 2021 HANYANG UNIVERSITY.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.