Browsing by Author "Rousselet, G."
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- Functional expression of the human CHIP28 water channel in a yeast secretory mutantPublication . Laizé, Vincent; Rousselet, G.; Verbavatz, J. M.; Berthonaud, V.; Gobin, R.; Roudier, N.; Abrami, L.; Ripoche, P.; Tacnet, F.The temperature-sensitive Saccharomyces cerevisiae mutant strain NY17, deficient in the secretory pathway (sec6-4 mutation), is used for the heterologous expression of the human CHIP28 water channel. After a heat-shock, the protein is present in partially purified post-golgi secretory vesicles, lmmunodetection and water transport studies, directly made on the vesicles, showed that CHIP28 is highly expressed and active in the yeast membranes.
- Molecular and functional study of AQY1 from Saccharomyces cerevisiae: role of the C-terminal domainPublication . Laizé, Vincent; Gobin, R.; Rousselet, G.; Badier, C.; Hohmann, S.; Ripoche, P.; Tacnet, F.The yeast YPR192w gene, which encodes a protein (Aqy1p) with strong homology to aquaporins (AQPs), was cloned from nine S. cerevisiae strains. The osmotic water permeability coefficient (Pf) of X. laevis oocytes expressing the gene cloned from the S1278b strain (AQY1-1) was 5.7 times higher than the Pf of oocytes expressing the gene cloned from other strains (AQY1-2). Aqy1-1p, initially cloned without its C-terminus (Aqy1-1DCp), mediated an ;3 times higher water permeability than the full-length protein. This corresponds to a 3-fold higher protein density in the oocyte plasma membrane, as shown by freeze-fracture electron microscopy. Pf measurements in yeast spheroplasts confirmed the presence of functional water channels in S1278b and a pharmacological study indicated that this strain contains at least a second functional aquaporin.