Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Analysis of Squalene Synthase Expression During the Development of Ganoderma lucidum

  • Zhao, M.W. (Microbiology Department, Nanjing Agricultural University, Key Laboratory of Microbiological Engineering of Agricultural Environment, Ministry of Agriculture) ;
  • Zhong, J.Y. (Microbiology Department, Nanjing Agricultural University, Key Laboratory of Microbiological Engineering of Agricultural Environment, Ministry of Agriculture) ;
  • Liang, W.Q. (Agro-Biotech Research Center, Agricultural Academy of Shanghai, Key Laboratory of Agriculture Genetics and Breeding of Shanghai) ;
  • Wang, N. (Agricultural Academy of Shanghai, Key Laboratory of Edible Fungus Genetics and Breeding Edible Fungi Institute, Ministry of Agriculture, Key Laboratory of Agriculture Genetics and Breeding of Shanghai) ;
  • Chen, M.J. (Agricultural Academy of Shanghai, Key Laboratory of Edible Fungus Genetics and Breeding Edible Fungi Institute, Ministry of Agriculture, Key Laboratory of Agriculture Genetics and Breeding of Shanghai) ;
  • Zhang, D.B. (Agro-Biotech Research Center, Agricultural Academy of Shanghai, Key Laboratory of Agriculture Genetics and Breeding of Shanghai) ;
  • Pan, Y.J. (Agricultural Academy of Shanghai, Key Laboratory of Edible Fungus Genetics and Breeding Edible Fungi Institute, Ministry of Agriculture, Key Laboratory of Agriculture Genetics and Breeding of Shanghai) ;
  • Jong.S.C. (American Type Culture Collection, 10801 University Boulevard)
  • Published : 2004.02.01
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Abstract

The medicinal properties of Ganoderma lucidum have been recognized in China for many centuries. Active pharmaceutical components include triterpenes. To elucidate the molecular regulation of triterpene biosynthesis in this mushroom, a 57-base pair DNA fragment encoding the fourth conserved domain SQ-4 (SMGLFLQKTNIIRDYNEDL) of squalene synthase was synthesized and cloned into the expression vector pET-32a(＋). The recombinant fusion protein induced by IPTG (isopropyl-$\beta$-D-thiogalactopyranoside) was overexpressed in the Escherichia coli. Using the purified recombinant fusion protein of 20.9 kDa, a specific polyclonal antibody was obtained from immunized rabbit. Expression of squalene synthase at different development stages of Ganoderma lucidum was analyzed.

Keywords

References

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