US EPA

1251023 

Journal Article 

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

Song, JA; Lee, DS; Park, JS; Han, KY; Lee, J 

2011 

Yes 

Enzyme and Microbial Technology
ISSN: 0141-0229 

49 

2 

124-130 

English 

22112398 

10.1016/j.enzmictec.2011.04.013 

WOS:000293439100002 

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. 

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