title: Co-expression of human cytochrome b5 increases expression of cytochrome P450 3A4 in Escherichia coli by stabilizing mRNA.
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).
authors: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea. msdong@korea.ac.kr
authors: Mi-Sook
authors: MS
authors: Dong
authors: Sang-Bum
authors: SB
authors: Lee
authors: Hyun-Jung
authors: HJ
authors: Kim
mesh_terms: D051544:Cytochrome P-450 CYP3A / Q000096:biosynthesis* / Q000235:genetics; D015786:Cytochromes b5 / Q000096:biosynthesis* / Q000235:genetics; D004926:Escherichia coli; D015964:Gene Expression Regulation, Bacterial; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism
chemical_list: D012333:RNA, Messenger; D015786:Cytochromes b5; D051544:Cytochrome P-450 CYP3A; C510163:CYP3A4 protein, human