Purification and biophysical characterization of the AIMP2-DX2 protein
- Authors
- Jha, Roshan; Cho, Hye Young; Mushtaq, Ameeq Ui; Lee, Kiho; Kim, Dae Gyu; Kim, Sunghoon; Jeon, Young Ho
- Issue Date
- Apr-2017
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- AIMP2; DX2; Oncogenic; Dimer; NMR
- Citation
- PROTEIN EXPRESSION AND PURIFICATION, v.132, pp.131 - 137
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROTEIN EXPRESSION AND PURIFICATION
- Volume
- 132
- Start Page
- 131
- End Page
- 137
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/84021
- DOI
- 10.1016/j.pep.2017.02.002
- ISSN
- 1046-5928
- Abstract
- Besides their primary role in protein synthesis, aminoacyl-tRNA synthetases (AARSs) are involved in several non-canonical processes such as apoptosis, inflammation and angiogenesis through their interactions with various cellular proteins. Nine of these AARSs interact with three aminoacyl-tRNA synthetase interacting multifunctional proteins (AIMPs), forming a multi-synthetase complex (MSC) in eukaryotes. Among the three AIMPs, AIMP2 is involved in controlling cell proliferation and apoptosis. However, a splicing variant of AIMP2 lacking exon 2, referred to as AIMP2-DX2, is oncogenic and compromises the pro-apoptotic activity of AIMP2 by competing with it for p53 and TRAF2. AIMP2-DX2 is also an inhibitor of pl4arf activity. Thus, there is a pressing need for structural insight into the oncogenic role of AIMP2-DX2. In this study, we expressed and purified human AIMP2-DX2 using a SUMO tag to more than 95% purity and a yield of 10 mg/L. We have used size exclusion chromatography, glutaraldehyde cross-linking, dynamic light scattering and nuclear magnetic resonance spectroscopy to characterize its biophysical properties. These data indicate monomer-dimer equilibrium of AIMP2-DX2 in solution. These results form the basis for the structure-function study of oncogenic AIMP2-DX2. (C) 2017 Elsevier Inc. All rights reserved.
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