A novel Escherichia coli solubility enhancer protein for fusion expression of aggregation-prone heterologous proteins

Jong Am Song, Dae Sung Lee, Jin Seung Park, Kyung Yeon Han, Jeewon Lee

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Through the proteome analysis of Escherichia coli BL21(DE3), we previously identified the stress-responsive protein, arsenate reductase (ArsC), that showed a high cytoplasmic solubility and a folding capacity even in the presence of stress-inducing reagents. In this study, we used ArsC as an N-terminal fusion partner to synthesize nine aggregation-prone proteins as water-soluble forms. As a result, solubility of the aggregation-prone proteins increased dramatically by the fusion of ArsC, due presumably to its tendency to facilitate the folding of target proteins. Also, we evaluated and confirmed the efficacy of ArsC-fusion expression in making the fusion-expressed target proteins have their own native function or structure. That is, the self-assembly function of human ferritin light chain, l-arginine-degrading function of arginine deiminase, and the correct secondary structure of human granulocyte colony stimulating factor were clearly observed through transmission electron microscope analysis, colorimetric enzyme activity assay, and circular dichroism, respectively. It is strongly suggested that ArsC can be in general an efficient fusion expression partner for the production of soluble and active heterologous proteins in E. coli.

Original languageEnglish
Pages (from-to)124-130
Number of pages7
JournalEnzyme and Microbial Technology
Volume49
Issue number2
DOIs
Publication statusPublished - 2011 Jul 10

    Fingerprint

Keywords

  • ArsC
  • Escherichia coli BL21(DE3)
  • Folding enhancer
  • Fusion partner
  • Proteome
  • Stress-resistant protein

ASJC Scopus subject areas

  • Biochemistry
  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this