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Topology of membrane insertion in vitro and plasma membrane assembly in vivo of the yeast arginine permease
Author(s) -
Ahmad M.,
Bussey H.
Publication year - 1988
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1988.tb00071.x
Subject(s) - permease , biology , endoplasmic reticulum , biochemistry , membrane topology , vesicle associated membrane protein 8 , membrane transport protein , membrane contact site , membrane protein , arginine , glycosylation , phosphatase , microbiology and biotechnology , integral membrane protein , amino acid , membrane , gene , enzyme , transporter
Summary We have examined the topology of the yeast arginine permease, a plasma‐membrane protein with multiple membrane‐spanning domains. Using fusions of the permease with the glycosylatable secreted yeast protein, acid phosphatase, we identified membrane‐spanning sequences that can translocate adjacent acid phosphatase across the membrane of the endoplasmicreticulum (ER), as measured by in vitro glycosylation. Examination for the presence or absence ofglycosylation in a systematic series of such fusions gave an internally consistent model for the lumenat orcytoplasmic disposition of the acid phosphatase reporter, defining the topology of the permease. The phenotypes of a further set of arginine permease gene fusions with portions of the gene for the secreted protein, killer toxin, suggest that the pathways of export of membrane and secreted proteins need not be functionally distinct.