Highly efficient folding of multi-disulfide proteins in superoxidizing Escherichia coli cytoplasm

Biotechnol Bioeng. 2014 Dec;111(12):2520-7. doi: 10.1002/bit.25309. Epub 2014 Aug 5.

Abstract

In this study, we monitored the thiol-disulfide redox potential of different Escherichia coli strains using redox-sensitive variants of green fluorescent protein. The cells with extreme oxidizing cytoplasm were generated by introducing a highly efficient disulfide relay system. The developed cells have exceptionally efficient de novo disulfide bond formation and significantly improve the oxidative folding of the client multi-disulfide proteins. Superoxidizing E. coli strain provides an effective method for the high-level production of recombinant disulfide-containing proteins.

Keywords: disulfide formation; oxidative protein folding; redox potential; superoxidizing cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cytoplasm / chemistry
  • Cytoplasm / metabolism*
  • Disulfides / chemistry
  • Disulfides / metabolism*
  • Escherichia coli / chemistry
  • Escherichia coli / cytology
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • Oxidation-Reduction
  • Oxidoreductases Acting on Sulfur Group Donors
  • Protein Folding
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism

Substances

  • Disulfides
  • Escherichia coli Proteins
  • Recombinant Fusion Proteins
  • Oxidoreductases Acting on Sulfur Group Donors