Browse > Article

Expression and Purification of Unstructured Protein, IMUP-1, using Chaperone Co-expression System for NMR Study  

Yi, Jong-Jae (College of pharmacy, CHA University)
Yoo, Jung Ki (College of pharmacy, CHA University)
Kim, Jin Kyeoung (College of pharmacy, CHA University)
Son, Woo Sung (College of pharmacy, CHA University)
Publication Information
Journal of the Korean Magnetic Resonance Society / v.17, no.1, 2013 , pp. 30-39 More about this Journal
Immortalization-upregulated protein-1 (IMUP-1) genes have been cloned and are known to be involved in SV40-mediated immortalization. IMUP-1 gene is highly expressed in various cancer cell lines and tumors, suggesting the possibility that they might be involved in tumorigenicity. Previously, there were several problems for overexpression of IMUP-1 in bacterial expression systems including low solubility and aggregation due to unstructured property. To investigate the structural properties, it is necessary to obtain lots of pure and soluble proteins. Accordingly, the co-expression systems of bacterial chaperone proteins, GroEL-GroES, were used to increase solubility of IMUP-1. From the analysis of NMR and CD experiment data, it is suggested that the protein adopt typical the random coil properties in solution.
IMUP-1; Chaperone; Purification; CD; NMR;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Jha, K. K., Banga, S., Palejwala, V., Ozer, H. L. Exp. Cell Res. 245, 1. (1998).   DOI   ScienceOn
2 Wright, W. E., Pereira-Smith, O. M., Shay, J. W. Mol. Ell. Biol. 9, 3088. (1989).
3 Reddel, R. R. Ann. New York Acad. Sci. 854, 8. (1998).   DOI
4 Powell, A. J., Darmon, A. J., Gonos, E. S., Lan, E. W., Peden, K. W., Jat, P. S. Oncogene. 18, 7343. (1999).   DOI
5 Hayflick, L., Moorhead, P. S. Cell Res. 25, 585. (1961).   DOI   ScienceOn
6 Hayflick, L. Cell Res. 37, 614. (1965).   DOI   ScienceOn
7 J. K. Kim, R. Roland, I. Yoshiko, K. Seishi. Gene. 257, 327. (2000).   DOI   ScienceOn
8 Z. Y. Ryoo, B. K. Jung, S. R. Lee, M. O. Kim, S. H. Kim, H. J. Kim, J. Y. Ahn, T. H. Lee, Y. H. Cho, J. H. Park, J. K. Kim. Biochem Biophys Res Commun. 349, 995. (2006).   DOI   ScienceOn
9 J. K. Kim, H. J. An, N. K. Kim, J. Y. Ahn, K. S. Kim, Y. J. Kang, J. J. Ko, D. Oh, C. Lee, S. J. Kim, K. Y. Cha. Anticancer Res. 23, 4709. (2003).
10 Cortazzo, P., Cervenansky, C., Marin, M., Reiss, C., Ehrlich, R., & Deana, A. Biochemical and Biophysical Research Communications. 293, 537. (2002).   DOI   ScienceOn
11 Johnson, J. L., & Craig, E. A. Cell. 90,201. (1997)..   DOI   ScienceOn
12 Horwich, A. L., Low, K. B., Fenton, W. A., Hirshfield, I. N., & Furtak, K Cell. 74, 909. (1993).   DOI   ScienceOn
13 Hartl, F. U. Nature. 381, 571. (1996).   DOI   ScienceOn
14 Hartl, F. U., & hayer-Hartl, M. Science. 295, 1852. (2002).   DOI   ScienceOn
15 Fenton, W. A., & Horwich, A. L. Science. 6, 743. (1997).
16 Brain, K., Otwinowdki, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., et al. Nature. 371, 578. (1994).   DOI   ScienceOn
17 Hunt, J. F., Weaver, A. J., Landry, S. J., Gierash, L., & Deisenhofer, J. Nature. 379, 37. (1996).   DOI   ScienceOn
18 Xu, Z., Horwich, A. L., & Sigler, P. B. Nature. 388, 741. (1997).   DOI   ScienceOn
19 Jonathan, S. W., Hays, S. R., Wayne, A. F., Joseph, M. B., Arthur, L. H. Cell Press. 84, 481. (1996).
20 Garnier, J., Garnier, J. F., Robson, B., R. F. Doolittle, Editor. 266, 540. (1996).   DOI   ScienceOn
21 Dosztanyi, Z., Csizmok, V., Tompa, P. and Simon, I. J. Mol. Biol. 347, 827. (2005).   DOI   ScienceOn
22 Nishihara, K., Kanemori, M., Yanagi, H., & Yura, Y. Applied and Environmental Microbiology. 66, 884. (2000).   DOI   ScienceOn
23 Delaglio, F., et al., J. Biomol. NMR. 6(3), 277. (1995).
24 Johnson, B. A. and R. A. Blevins, J. Biomol. Nmr. 4(5), 603. (1994).   DOI   ScienceOn
25 P. Goloubinoff, A. A. Gatenby, and G. H. Lorimer, Nature. 337, 44. (1989).   DOI   ScienceOn
26 Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, Marc R., Appel, Ron. D., Bairoch, A., J. M. Walker, Editor. Humana Press. 52,571.(2005).