title: Escherichia coli EDA is a novel fusion expression partner to improve solubility of aggregation-prone heterologous proteins.
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.
authors.affiliation: Department of Chemical and Biological Engineering, Korea University, Anam-Dong 5-1, Seongbuk-Gu, Seoul 136-713, Republic of Korea. Electronic address: yoonsik89@korea.ac.kr.
authors.forename: Yoon-Sik
authors.initials: YS
authors.lastname: Kang
authors.affiliation: SolGent Co., Ltd. Plant and Biomedical Research Institute, 43-10, Techno 5-ro, Yuseong-Gu, Daejeon 305-504, Republic of Korea. Electronic address: uga33@korea.ac.kr.
authors.forename: Jong-Am
authors.initials: JA
authors.lastname: Song
authors.affiliation: Emerging Technology Research Center, Corporate Technology Operations SAIT, Samsung Electronics Co., Ltd., Giheung-gu, Yongin-si, Gyeonggi-do, Republic of Korea. Electronic address: ruddus78@korea.ac.kr.
authors.forename: Kyung-Yeon
authors.initials: KY
authors.lastname: Han
authors.affiliation: Department of Chemical and Biological Engineering, Korea University, Anam-Dong 5-1, Seongbuk-Gu, Seoul 136-713, Republic of Korea. Electronic address: leejw@korea.ac.kr.
authors.forename: Jeewon
authors.initials: J
authors.lastname: Lee
mesh_terms: D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D012995:Solubility
chemical_list: D029968:Escherichia coli Proteins
keywords: Escherichia coli BL21; KDPG aldolase (EDA); Proteome; Solubility enhancer; Stress-responsive protein