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An Efficient Method for the Expression and Reconstitution of Thermostable Mn/Fe Superoxide Dismutase from Aeropyrum pernix K1

  • Lee, Hee-Jin (Department of Chemistry, College of Natural Sciences, Chung-Ang University) ;
  • Kwon, Hye-Won (Department of Chemistry, College of Natural Sciences, Chung-Ang University) ;
  • Koh, Jong-Uk (Department of Chemistry, College of Natural Sciences, Chung-Ang University) ;
  • Lee, Dong-Kuk (Department of Fine Chemistry, Seoul National University of Technology) ;
  • Moon, Ja-Young (Department of Biochemistry, College of Natural Sciences, Changwon National University) ;
  • Kong, Kwang-Hoon (Department of Chemistry, College of Natural Sciences, Chung-Ang University)
  • 투고 : 2009.11.04
  • 심사 : 2009.12.21
  • 발행 : 2010.04.28

초록

The gene APE0743 encoding the superoxide dismutase (ApSOD) of a hyperthermophilic archaeon Aeropyrum pernix K1 was cloned and overexpressed as a GST fusion protein at a high level in Escherichia coli. The expressed protein was simply purified by the process of glutathione affinity chromatography and thrombin treatment. The ApSOD was a homodimer of 25 kDa subunits and a cambialistic SOD, which was active with either Fe(II) or Mn(II) as a cofactor. The ApSOD was highly stable against high temperature. This thermostable ApSOD is expected to be applicable as a useful biocatalyst for medicine and bioindustrial processes.

키워드

참고문헌

  1. Beyer, W. F., J. A. Jr. Reynolds, and I. Fridovich. 1989. Differences between the manganese and the iron-containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies. Biochemistry 28: 4403-4409. https://doi.org/10.1021/bi00436a042
  2. Fridovich, I. 1986. Superoxide dismutases. Adv. Enzymol. 58: 61-97.
  3. Grace, S. C. 1990. Phylogenetic distribution of superoxide dismutase supports an endosymbiotic origin for chloroplasts and mitochondria. Life Sci. 47: 1875-1886. https://doi.org/10.1016/0024-3205(90)90399-C
  4. Lee, S. H., S. Y. Kim, D. W. Kim, S. H. Jang, S.-S. Lim, H. J. Kwon, et al. 2008. Actve component of Fatsia japonica enhances the transduction efficiency of tat-SOD fusion protein both in vitro and in vivo. J. Microbiol. Biotechnol. 18: 1613-1619.
  5. Li, D.-C., J. Gao, Y.-L. Li, and J. Lu. 2005. A thermosable manganese-containing superoxide dismutase from the thermophilic fungus Thermomyces lanuginosus. Extremophiles 9: 1-6. https://doi.org/10.1007/s00792-004-0413-4
  6. Lim, J.-H., K. Y. Hwang, J. Choi, D. Y. Lee, B.-Y. Ahn, Y. Cho, K.-S. Kim, and Y. S. Han. 2001. Mutation effects on thermostable superoxide dismutase from Aquifex pyrophilus: Understanding the molecular basis of protein thermostability. Biochem. Biophys. Res. Commun. 288: 263-268. https://doi.org/10.1006/bbrc.2001.5752
  7. Parker, M. W. and C. C. Blake. 1988. Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett. 229: 377-382. https://doi.org/10.1016/0014-5793(88)81160-8
  8. Sako, Y., N. Nomura, A. Uchida, Y. Ishida, H. Morii, Y. Koga, T. Hoaki, and T. Maruyama. 1996. Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C. Int. J. Syst. Bacteriol. 46: 1070-1077. https://doi.org/10.1099/00207713-46-4-1070
  9. Sato, S. and J. I. Harris. 1977. Superoxide dismutase from Thermus aquaticus. Eur. J. Biochem. 73: 373. https://doi.org/10.1111/j.1432-1033.1977.tb11328.x
  10. Sehn, A. P. and B. Meier. 1994. Regulation of an in vivo metal-exchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors. Biochem. J. 304: 803-808.
  11. Shijin, E., F. Guo, S. Liu, J. Chen, Y. Wang, and D. Li. 2007. Purification, characterization, and molecular cloning of a thermostable superoxide dismutase from Thermoascus aurantiacus. Biosci. Biotechnol. Biochem. 71: 1090-1093. https://doi.org/10.1271/bbb.60709
  12. Slykhouse, T. O. and J. A. Fee. 1976. Physical and chemical studies on bacterial superoxide dismutases. J. Biol. Chem. 251: 5472-5477.
  13. Weisiger, R. A. and I. Fridovich. 1973. Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial localization. J. Biol. Chem. 248: 4793-4796.
  14. Whittaker, J. W. 1997. A model for local melting of metalloprotein structure. J. Phys. Chem. B 101: 674-677. https://doi.org/10.1021/jp963049t
  15. Yamano, S., Y. Sako, N. Nomura, and T. Maruyama. 1999. A cambialistic SOD in a strictly aerobic hyperthermophilic archaeon, Aeropyrum pernix. J. Biochem. 126: 218-225. https://doi.org/10.1093/oxfordjournals.jbchem.a022426
  16. Youn, H. D., E. J. Kim, J. H. Roe, Y. C. Hah, and S. O. Kang. 1996. A novel nickel-containing superoxide dismutase from Streptomyces spp. Biochem. J. 318: 889-896.

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  1. SORGOdb: Superoxide Reductase Gene Ontology curated DataBase vol.11, pp.None, 2010, https://doi.org/10.1186/1471-2180-11-105
  2. Crystal structure of the cambialistic superoxide dismutase from Aeropyrum pernix K1 – insights into the enzyme mechanism and stability vol.278, pp.4, 2010, https://doi.org/10.1111/j.1742-4658.2010.07977.x
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