Biotechnology Letters

, Volume 31, Issue 10, pp 1589–1593

Enhanced bacterial expression of several mammalian cytochrome P450s by codon optimization and chaperone coexpression

Authors

    • Chengdu Institute of BiologyChinese Academy of Sciences
  • Jing Qiao
    • Chengdu Institute of BiologyChinese Academy of Sciences
    • Graduate School of the Chinese Academy of Sciences
  • Zhi-Gang Zhang
    • Chengdu Institute of BiologyChinese Academy of Sciences
    • Graduate School of the Chinese Academy of Sciences
  • F. Peter Guengerich
    • Department of Biochemistry, Center in Molecular ToxicologyVanderbilt University School of Medicine
  • Yan Liu
    • Chengdu Institute of BiologyChinese Academy of Sciences
  • Xiao-Qiong Pei
    • Chengdu Institute of BiologyChinese Academy of Sciences
Original Research Paper

DOI: 10.1007/s10529-009-0059-5

Cite this article as:
Wu, Z., Qiao, J., Zhang, Z. et al. Biotechnol Lett (2009) 31: 1589. doi:10.1007/s10529-009-0059-5

Abstract

To elucidate the effects of codon optimization and chaperone coexpression on the heterologous expression of mammalian cytochrome P450s (P450) in Escherichia coli, the expression of P450s 2B1, 2S1, 2U1, 2W1, and 27C1 were investigated. With codon optimization for N-terminus or the entire gene, the expression levels of P450 27C1, 2U1 and 2W1 increased 22-fold, 3.6-fold and 2.1-fold, respectively, while those for P450s 2B1 and 2S1 remained unchanged. With coexpression of E. coli molecular chaperones GroEL/ES, the expression level increased up to 14-fold for P450 27C1, and 3- to 5-fold for P450s 2B1, 2S1, and 2W1. Simultaneous application of these two techniques resulted in synergetic effects.

Keywords

ChaperonCodonCytochrome P450Escherichia coliExpression

Supplementary material

10529_2009_59_MOESM1_ESM.doc (244 kb)
(DOC 244 kb)

Copyright information

© Springer Science+Business Media B.V. 2009