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트립토판 합성효소 α 소단위체의 다양한 단백질 덩어리 형성

Various Aggregate Forms of Tryptophan Synthase α-Subunit

  • 박명원 (부산대학교 자연과학대학 분자생물학과) ;
  • 임운기 (부산대학교 자연과학대학 분자생물학과)
  • Park, Myung Won (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Lim, Woon Ki (Department of Molecular Biology, College of Natural Sciences, Pusan National University)
  • 투고 : 2013.01.15
  • 심사 : 2013.01.26
  • 발행 : 2013.02.28

초록

단백질 덩어리는 질환의 원인이 되기도 하고, 유용한 유전자 재조합 단백질의 생산시 문제를 야기하기도 한다. 본 연구에서는 조건을 달리함으로 트립토판 합성효소 ${\alpha}$ 소단위체로부터 적어도 3가지 이상 다른 종류의 덩어리가 생길 수 있음을 보여주고 있다; (1) 불투명 흰색 침전 가능한 덩어리 (2) 투명하고 겔 유형의 침전 가능한 덩어리 (3) 불침전 덩어리. 이런 다른 종류의 덩어리 형태는 다른 기작을 통해 일어날 것으로 추정된다.

Protein aggregation can cause diseases and hinder the production of useful recombinant proteins. The present study showed that at least three types of aggregates can be formed from tryptophan synthase ${\alpha}$-subunit (${\alpha}TS$) by varying conditions: (1) an opaque white precipitous aggregate, (2) a transparent gel-like precipitous aggregate, and (3) an unprecipitous aggregate. Macroscopically different aggregate types might suggest different mechanisms underlying aggregation processes.

키워드

참고문헌

  1. Bennett, M. J., Sawaya, M. R. and Eisenberg, D. 2006. Deposition diseases and 3D domain swapping. Structure 14, 811-824. https://doi.org/10.1016/j.str.2006.03.011
  2. Chiti, F., Taddei, N., Baroni, F., Capanni, C., Stefani, M., Ramponi, G. and Dobson, C. M. 2002. Kinetic partitioning of protein folding and aggregation. Nature Struct Biol 9, 137-143. https://doi.org/10.1038/nsb752
  3. Davis, B. J. 1964. Disc electrophoresis II. Method and application to human serum proteins. Ann N Y Acad Sci 121, 404-427.
  4. Gast, K., Zirwer, D., Muller-Frohne, M. and Damaschun, G. 1999. Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A. Protein Sci 8, 625-634.
  5. Jeong, M. S., Jeong, J. K., Park, K. S., Kim, H. T., Lee, K. M., Lim, W. K. and Jang, S. B. 2004. Crystallization and preliminary X-ray analysis of tryptophan synthase ${\alpha}$-subunits from Escherichia coli. Acta Crystallogr D Biol Crystallogr 60, 132-134. https://doi.org/10.1107/S0907444903022935
  6. Kim, J. W., Kim, E. Y., Park, H. H., Jung, J. E., Kim, H. D., Shin, H. J. and Lim, W. K. 2001. Homodimers of mutant tryptophan synthase ${\alpha}$-subunits in Escherichia coli. Biochem Biophys Res Commun 289, 568-572. https://doi.org/10.1006/bbrc.2001.6022
  7. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. https://doi.org/10.1038/227680a0
  8. Leggett-Bailey, J. 1962. Techniques in Protein Chemistry. Elsevier Scientific Publishing Co. New York.
  9. Lim, W. K., Shin, H. J., Milton, D. L. and Hardman, J. K. 1991. Relative activities and stabilities of mutant Escherichia coli tryptophan synthase ${\alpha}$-subunits. J Bacteriol 173, 1886-1893.
  10. Nishio, K., Morimoto, Y., Ishizuka, M., Ogasahara, K., Tsukihara, T. and Yutani, K. 2005. Conformational changes in the ${\alpha}$-subunit coupled to binding of the ${\beta}_2$-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase ${\alpha}$-subunit alone. Biochem 44, 1184-1192. https://doi.org/10.1021/bi047927m
  11. Park, W. P., Jeong, J. K., Shin, H. J. and Lim, W. K. 2003. Effect of temperature and urea on in vitro aggregation of tryptophan synthase ${\alpha}$-subunits. J Biomed Lab Sci 9, 203-207.
  12. Schonbrunner, N., Wey, J., Engels, J., Georg, H. and Kiefhaber, T. 1996. Native-like ${\beta}$-structure in a trifluoroethanol- induced partially folded state of the all-${\beta}$-sheet protein tendamistat. J Mol Biol 260, 432-445. https://doi.org/10.1006/jmbi.1996.0412
  13. Warren, J. D., Fletcher, P. D. and Golden, H. L. 2012. The paradox of syndromic diversity in Alzheimer disease. Nat Rev Neurol 8, 451-464.
  14. Wu, Y., Kondrashkina, E., Kayatekin, C., Matthews, C. R. and Bilsel, O. 2009. Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein. Proc Natl Acad Sci USA 105, 13367-13372.