Membrane Topology of NADPH–Cytochrome P450 Reductase on the Endoplasmic Reticulum

Topology of the membrane-anchoring segment of mouse NADPH–cytochrome P450 reductase in the endoplasmic reticulum membrane was elucidated. An N-glycosylation site was generated in the amino-terminal hydrophilic sequence of the reductase, and the mutated protein was expressed in a cell-free system in...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 1998-03, Vol.351 (2), p.175-179
Main Authors: Kida, Yuichiro, Ohgiya, Satoru, Mihara, Katsuyoshi, Sakaguchi, Masao
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
endoplasmic reticulum
Endoplasmic Reticulum - enzymology
Glycosylation
membrane integration
Membrane Proteins - chemistry
Mice
Molecular Sequence Data
Mutagenesis - genetics
NADH, NADPH Oxidoreductases - chemistry
NADPH-Ferrihemoprotein Reductase
Plasmids - genetics
Protein Biosynthesis - genetics
Signal Recognition Particle - physiology
signal-anchor sequence
topology
Triticum - enzymology
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Summary:Topology of the membrane-anchoring segment of mouse NADPH–cytochrome P450 reductase in the endoplasmic reticulum membrane was elucidated. An N-glycosylation site was generated in the amino-terminal hydrophilic sequence of the reductase, and the mutated protein was expressed in a cell-free system in the presence of microsomal vesicles. Thein vitrosynthesized reductase protein was integrated into the microsomal membrane and N-glycosylated depending on the presence of signal recognition particles. We conclude that the amino-terminal membrane-anchoring segment of the reductase is a type I signal-anchor sequence which shows amino-terminus-lumen and carboxy-terminus-cytoplasm topology.
ISSN:0003-9861
1096-0384
DOI:10.1006/abbi.1997.0553