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Progression of the stacked Golgi compartments in the yeast Saccharomyces cerevisiae by overproduction of GDP–mannose transporter
Author(s) -
Hashimoto Hitoshi,
Abe Masato,
Hirata Aiko,
Noda Yoichi,
Adachi Hiroyuki,
Yoda Koji
Publication year - 2002
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.925
Subject(s) - golgi apparatus , biology , saccharomyces cerevisiae , vacuole , cytoplasm , mannose , microbiology and biotechnology , transport protein , biochemistry , cellular compartment , secretory pathway , yeast , endoplasmic reticulum , cell
The Golgi compartments of the yeast Saccharomyces cerevisiae are dispersed within the cytoplasm, in contrast to the stacked cisternae in the mammalian cell, and consequently are observed as a punctate pattern by immunofluorescent staining of Golgi‐marker proteins. The VIG4/VRG4 gene encodes the essential yeast GDP–mannose transporter, which is a polytopic membrane protein in the early and medial Golgi compartments. Upon overexpression of this gene by the aid of a strong promoter and multicopy vector, we found that stacked multivesicular structures, which resembled the cisternae of mammalian Golgi apparatus, had developed in S. cerevisiae . Immuno‐electron microscopy showed that the GDP–mannose transporter was located on the stacked cisternae. Immuno‐isolation and immunoblotting analyses of the vesicles showed that the overproduced GDP–mannose transporter also co‐localized with the Golgi glycosyltransferases, but not with the ER‐ or late Golgi‐marker proteins as in the control cell. We propose that the localization mechanism of the GDP–mannose transporter in the Golgi compartment would be efficient and hardly saturable, and therefore the overproduced protein induced a progression of Golgi‐like compartments rather than being mislocalized in other compartments, such as the ER or a vacuole. Copyright © 2002 John Wiley & Sons, Ltd.