Overexpression of the ER-membrane protein P-450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae Journal Article


Authors: Wiedmann, B.; Silver, P.; Schunck, W. H.; Wiedmann, M.
Article Title: Overexpression of the ER-membrane protein P-450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae
Abstract: High expression of microsomal cytochrome P-450 CYP52A3 from Candida maltosa induces the formation of membrane stacks in Saccharomyces cerevisiae. Membrane proliferation is accompanied by coinduction of the ER proteins KAR2p and SEC61p and accumulation of precursor forms of proteins that have to translocate across the ER membrane (KAR2p, α factor). Cytosolic proteins (SSA1p and 2p) and mitochondrial proteins (CYT c1p and F1βp) are not affected. N-terminal truncated P-450 proteins remain in the cytoplasm and fail to induce membrane proliferation, KAR2p/SEC61p expression, and precursor accumulation. Membrane and precursor protein accumulation are typical features of sec mutants. We assume that the high amounts of P-450p block one or more factor(s) of the transport machinery and thereby cause the observed phenomena. © 1993.
Keywords: nonhuman; mutant protein; gene expression; membrane proteins; endoplasmic reticulum; amino acid sequence; saccharomyces cerevisiae; membrane protein; plasmids; glucose; fungi; cytochrome p450; intracellular membranes; candida; restriction mapping; fungus mutant; galactose; cytochrome p-450 enzyme system; microsomes; colocalization; priority journal; article; coinduction; cytochrome p-450; kar2p; membrane proliferation; sec61p; candida maltosa
Journal Title: Biochimica et Biophysica Acta (BBA) - Biomembranes
Volume: 1153
Issue: 2
ISSN: 0005-2736
Publisher: Elsevier B.V.  
Date Published: 1993-12-12
Start Page: 267
End Page: 276
Language: English
DOI: 10.1016/0005-2736(93)90415-v
PUBMED: 8274497
PROVIDER: scopus
DOI/URL:
Notes: Source: Scopus
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