Proteolysis and synthetic strategy of human G-CSF in Escherichia coli BL21 (DE3)
- Authors
- Song, Jong-Am; Han, Kyung-Yeon; Ahn, Keum-Young; Park, Jin-Seung; Seo, Hyuk-Seong; Lee, Jeewon
- Issue Date
- 8-7월-2009
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- Human granulocyte colony-stimulating factor (hG-CSF); E. coli BL21(DE3); N-terminal fusion partner; C-terminal proteolysis
- Citation
- ENZYME AND MICROBIAL TECHNOLOGY, v.45, no.1, pp.7 - 14
- Indexed
- SCIE
SCOPUS
- Journal Title
- ENZYME AND MICROBIAL TECHNOLOGY
- Volume
- 45
- Number
- 1
- Start Page
- 7
- End Page
- 14
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/119678
- DOI
- 10.1016/j.enzmictec.2009.02.010
- ISSN
- 0141-0229
- Abstract
- We report for the first time that the C-terminal region of hG-CSF suffers from proteolytic degradation when human granulocyte colony-stimulating factor (hG-CSF) is directly expressed in Escherichia coli BL21 (DE3). It is believed that the rapid proteolysis occurs at the C-terminus of hG-CSF that is very easily exposed to E. coli protease(s) during a short period following protein synthesis and prior to completion of the formation of the inclusion body. The recombinant hG-CSF that is expressed with an N-terminal fusion partner is effectively protected from the proteolysis. It seems that since the N-terminus of hG-CSF is located very close to the C-terminus, the presence of the N-terminal fusion partner masks the C-terminal region of hG-CSF and protects it from proteolytic degradation by E. coli protease(s). Furthermore, the solubility of hG-CSF markedly increased in E coli cytoplasm when a stress-responsive and aggregation-resistant protein, i.e. aspartate carbamoyl-transferase catalytic chain (PyrB) Was used as a novel N-terminal fusion partner proteins. (C) 2009 Elsevier Inc. All rights reserved.
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