Proliferation of intracellular membrane structures upon homologous overproduction of cytochrome P-450 in Candida maltosa.
In an alkane-assimilating yeast, Candida maltosa, a cultivation on alkane causes both induction of endoplasmic reticulum (ER)-resident membrane proteins, such as cytochrome P-450, and proliferation of ER. In this study, individual genes for alkane-inducible forms of cytochrome P-450 (P-450alk) were homologously overexpressed in C. maltosa using a galactose-inducible expression system developed in this yeast. Immunoelectron microscopy revealed that, upon the overexpression, a dramatic proliferation of ER occurred, in which overproduced P-450alk protein accumulated. The proliferated membranes were mainly tubular forms and stacks of paired membranes were also observed after prolonged expression. The tubular forms were morphologically very similar to the proliferated ER in alkane-induced C. maltosa cells. The observed proliferation of ER membranes by homologous overproduction of P-450alk, here depicted, will provide a unique opportunity for investigating the mechanisms by which cells regulate ER biogenesis, in comparison with the intrinsic form of ER proliferation.
Ohkuma
M
M
Department of Agricultural Chemistry, University of Tokyo, Japan.
Park
S M
SM
Zimmer
T
T
Menzel
R
R
Vogel
F
F
Schunck
W H
WH
Ohta
A
A
Takagi
M
M
D002175:Candida / Q000201:enzymology*; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis*; D004721:Endoplasmic Reticulum / Q000378:metabolism / Q000648:ultrastructure; D005822:Genetic Vectors; D007425:Intracellular Membranes / Q000378:metabolism; D008565:Membrane Proteins / Q000096:biosynthesis; D016253:Microscopy, Immunoelectron
D008565:Membrane Proteins; D003577:Cytochrome P-450 Enzyme System