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Escherichia coli EDA is a novel fusion expression partner to improve solubility of aggregation-prone heterologous proteins

Kang, Y.-S.; Song, J.-A.; Han, K.-Y.; Lee, J.

Journal of Biotechnology 194: 39-47

2015


ISSN/ISBN: 1873-4863
PMID: 25486632
DOI: 10.1016/j.jbiotec.2014.11.025
Accession: 057794655

Since the use of solubility enhancer proteins is one of the effective methods to produce active recombinant proteins within Escherichia coli, the development of a novel fusion expression partner that can be applied to various aggregation-prone proteins is of crucial importance. In our previous work, two-dimensional electrophoresis (2-DE) was employed to systematically analyze the E. coli BL21 (DE3) proteome profile in response to heat treatment, and KDPG aldolase (EDA) was identified as a heat-responsive and aggregation-resistant protein. When used as fusion expression partner, EDA significantly increased the solubility of seven aggregation-prone heterologous proteins in the E. coli cytoplasm. The efficacy of EDA as a fusion expression partner was evaluated through the analysis of bioactivity or secondary structure of several target proteins: EDA-fusion expression resulted in the synthesis of bioactive human ferritin light chain and bacterial arginine deiminase and the formation of correct secondary structure of human granulocyte colony stimulation factor.

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