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

Yoon Sik Kang, Jong Am Song, Kyung Yeon Han, Jeewon Lee

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)39-47
Number of pages9
JournalJournal of Biotechnology
Volume194
DOIs
Publication statusPublished - 2015 Jan 1

Keywords

  • Escherichia coli BL21
  • KDPG aldolase (EDA)
  • Proteome
  • Solubility enhancer
  • Stress-responsive protein

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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