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Expression and purification of a soluble ESX-binding core domain of sur2

Title
Expression and purification of a soluble ESX-binding core domain of sur2
Authors
Jeon K.-H.Jun K.-Y.Kim E.Y.Kwon Y.
Ewha Authors
권영주
SCOPUS Author ID
권영주scopus
Issue Date
2013
Journal Title
Preparative Biochemistry and Biotechnology
ISSN
1082-6068JCR Link
Citation
vol. 43, no. 4, pp. 364 - 375
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
For HER2 overexpression, the ESX transcription factor must interact with both the HER2 promoter and Sur2, a subunit of human mediator complex, using its Ets domain and transactivation domain, respectively. HER2 overexpression is a marker of poor prognosis in various types of cancers. Thus, interfering with the ESX-Sur2 interaction has been suggested as a novel strategy for the treatment of HER2 positive cancers. To design small molecule inhibitors against the ESX-Sur2 interaction, it is necessary to identify the structure of the interface of ESX-Sur2 binding. Therefore, in this study, we determined the optimal conditions for the overexpression and purification of a new version of Sur2, Sur2391-582, which was able to bind to ESX. To stabilize (His) 6-Sur2391-582, various different buffered conditions over a wide range of pH and ionic strengths were examined. The molecular mass of (His)6-Sur2391-582 was determined using mass spectroscopy and size exclusion chromatography. The purified (His)6-Sur 2391-582 protein displayed the same biological properties as that of the Sur2 full-length protein. © 2013 Taylor & Francis Group, LLC.
DOI
10.1080/10826068.2012.738273
Appears in Collections:
약학대학 > 약학과 > Journal papers
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