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

Paper ID Volume ID Publish Year Pages File Format Full-Text
17395 42666 2011 7 PDF Available
Title
A novel Escherichia coli solubility enhancer protein for fusion expression of aggregation-prone heterologous proteins
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.

Keywords
Fusion partner; ArsC; Folding enhancer; Stress-resistant protein; Escherichia coli BL21(DE3); Proteome
First Page Preview
A novel Escherichia coli solubility enhancer protein for fusion expression of aggregation-prone heterologous proteins
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 49, Issue 2, 10 July 2011, Pages 124–130
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering