Functional Analysis of the N -Terminal Transmembrane/signal -Anchor Sequence and Linker Domain of Cytochrome P450 2C2

Truncated forms of P450 2C2 lacking the N-terminal hydrophobic signal anchor sequence (Delta2- 20) or the signal anchor and linker region (Delta2-27) were expressed alone or as GFP fusions in E. coli and insect cells. The findings indicate that deletion of the signal anchor decreases assembly of P450 hemoprotein in E. coli but does not change the in vivo distribution of the protein. However, it alters the nature of membrane interaction such that P450 2C2 is no longer an integral membrane protein. Moreover, the results show that the linker domain is critical for the formation of functional P450 2C2 only when the P450 molecule is properly targeted and inserted in the membrane.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Microbiology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• D., Balraj

Contributors dc:contributor

• Kemper, Byron W.

• Biology, Molecular

Language dc:language

eng

Identifier

(MiAaPQ)AAI9955603

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/86753