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Co-expression of human cytochrome b(5) increases expression of cytochrome P450 3A4 in Escherichia coli by stabilizing mRNA

Authors
Dong, Mi-SookLee, Sang-BumKim, Hyun-Jung
Issue Date
May-2013
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Co-expression of CYP3A4; NADPH-cytochrome P450 reductase; Cytochrome b(5); mRNA stabilization; Stationary phase of E. coli
Citation
PROTEIN EXPRESSION AND PURIFICATION, v.89, no.1, pp.44 - 50
Indexed
SCIE
SCOPUS
Journal Title
PROTEIN EXPRESSION AND PURIFICATION
Volume
89
Number
1
Start Page
44
End Page
50
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/103463
DOI
10.1016/j.pep.2013.02.010
ISSN
1046-5928
Abstract
CYP3A4 is the most abundant cytochrome P450 in the human liver. The expression level of CYP3A4 when coexpressed with cytochrome b(5) (cyt b(5)) in Escherichia coli was 20-60% higher than that when it was expressed alone over an extended period (48-72 h). This time-dependent elevation in coexpression with cyt b(5) was a result of an increase in CYP3A4 mRNA half-life; no significant change in CYP3A4 degradation was seen in the bacterial protease fraction. These results suggest that the higher CYP3A4 levels observed upon coexpression with cyt b(5) primarily resulted from CYP3A4 mRNA stabilization by cyt b(5). (C) 2013 Elsevier Inc. All rights reserved.
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