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Synthesis of Mycoplasma arginine deiminase in E. coli using stress-responsive proteins

Authors
Ahn, Keum-YoungLee, BoramHan, Kyung-YeonSong, Jong-AmLee, Doo SungLee, Jeewon
Issue Date
9월-2014
Publisher
ELSEVIER SCIENCE INC
Keywords
Mycoplasma arginine deiminase; Stress-responsive protein; Solubility enhancer
Citation
ENZYME AND MICROBIAL TECHNOLOGY, v.63, pp.46 - 49
Indexed
SCIE
SCOPUS
Journal Title
ENZYME AND MICROBIAL TECHNOLOGY
Volume
63
Start Page
46
End Page
49
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/97493
DOI
10.1016/j.enzmictec.2014.05.004
ISSN
0141-0229
Abstract
We found Escherichia coli proteins, elongation factor Ts (Tsf), and malate dehydrogenase (Mdh) that can exist in the form of native and soluble proteins even under stress situation such as heat shock and protein denaturing condition. To examine their property as solubility enhancers, aggregation-prone Mycoplasma arginine deiminase (mADI), which has been suggested as anti-cancer agent, was fused to the C-terminal of each of them and cloned into pET28a to be expressed in the E. coli cytoplasm. When mADI was fused to fusion partners (Mdh, Tsf), a significant portion of the recombinant mADI was expressed in a soluble fraction (>90%) whereas the directly expressed mADI was aggregated to the inclusion body. In addition, recombinant mADI released from the fusion tag retained its soluble form and presented its specific enzymatic activity of converting L-arginine into citrulline (>10 Wing). These results show that Tsf and Mdh could serve as effective solubility enhancers for aggregation-prone proteins (e.g. mADI in this case) when used as fusion expression partners in bacterial expression systems. (C) 2014 Elsevier Inc. All rights reserved.
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공과대학 (화공생명공학과)
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