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J. Biol. Chem., Vol. 277, Issue 40, 37855-37862, October 4, 2002
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From the Ro09-0198 (Ro) is a tetracyclic peptide
antibiotic that binds specifically to phosphatidylethanolamine (PE) and
causes cytolysis. To investigate the molecular basis of transbilayer
movement of PE in biological membranes, we have isolated a series of
budding yeast mutants that are hypersensitive to the Ro peptide. One of the most sensitive mutants, designated ros3
(Ro-sensitive 3), showed no
significant change in the cellular phospholipid composition or in the
sensitivity to amphotericin B, a sterol-binding polyene macrolide
antibiotic. These results suggest that the mutation of ros3
affects the PE organization on the plasma membrane, rather than PE
synthesis or overall organization of the membrane structures. By
functional complementation screening, we identified the gene ROS3 affected in the mutant, and we showed that the
hypersensitive phenotype was caused by the defective expression of the
ROS3 gene product, Ros3p, an evolutionarily conserved
protein with two putative transmembrane domains. Disruption of the
ROS3 gene resulted in a marked decrease in the
internalization of fluorescence-labeled analogs of PE and
phosphatidylcholine, whereas the uptake of fluorescence-labeled phosphatidylserine and endocytic markers was not affected. Neither expression levels nor activities of ATP-binding cassette transporters of the ros3
A Novel Membrane Protein, Ros3p, Is Required for Phospholipid
Translocation across the Plasma Membrane in Saccharomyces
cerevisiae*
§,,,
,**
Department of Molecular Biodynamics, the
Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome,
Bunkyo-ku, Tokyo 113-8613, the § Department of Biology,
Faculty of Science, Ochanomizu University, 2-1-1 Ohtsuka,
Bunkyo-ku, Tokyo 112-8610, Supra-Biomolecular System Research
Group, RIKEN (Institute of Physical and Chemical Research), Frontier
Research System, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, and the
¶ Department of Biotechnology, the University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
cells differed from those of wild type
cells, suggesting that Ros3p is not related to the multidrug resistance
activities. Immunochemical analyses of the structure and subcellular
localization showed that Ros3p was a glycosylated membrane protein
localized in both the plasma membrane and the endoplasmic reticulum,
and that a part of Ros3p was associated with the detergent-insoluble glycolipid-enriched complexes. These results indicate that Ros3p is a
membrane glycoprotein that plays an important role in the phospholipid
translocation across the plasma membrane.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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