title: Aquaporins in Saccharomyces: Characterization of a second functional water channel protein.
abstract: The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2. Aqy1p has been shown to be a functional aquaporin in some strains, such as Sigma1278b. AQY2 is disrupted by a stop codon in most strains; however, Sigma1278b has an intact ORF. Because Sigma1278b Aqy2p has an intracellular localization in Xenopus oocytes and in yeast, other strains of yeast were examined. Aqy2p from Saccharomyces chevalieri has a single amino acid in the third transmembrane domain (Ser-141) that differs from Sigma1278b Aqy2p (Pro-141). S. chevalieri Aqy2p is a functional water channel in oocytes and traffics to the plasma membrane of yeast. The Sigma1278b parental strain, the aqy1-aqy2 double null yeast, and null yeast expressing S. chevalieri Aqy2p were examined under various conditions. Comparison of these strains revealed that the aquaporin null cells were more aggregated and their surface was more hydrophobic. As a result, the aquaporin null cells were more flocculent and more efficient at haploid invasive growth. Despite its primary intracellular localization, Sigma1278b Aqy2p plays a role in yeast similar to Aqy1p and S. chevalieri Aqy2p. In addition, Aqy1p and Aqy2p can affect cell surface properties and may provide an advantage by dispersing the cells during starvation or during sexual reproduction.
authors.affiliation: Departments of Biological Chemistry and Molecular Biology and Genetics, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.
authors.forename: J M
authors.initials: JM
authors.lastname: Carbrey
authors.forename: M
authors.initials: M
authors.lastname: Bonhivers
authors.forename: J D
authors.initials: JD
authors.lastname: Boeke
authors.forename: P
authors.initials: P
authors.lastname: Agre
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020346:Aquaporins / Q000235:genetics / Q000502:physiology*; D001483:Base Sequence; D002462:Cell Membrane / Q000502:physiology; D005260:Female; D016681:Genome, Fungal; D008969:Molecular Sequence Data; D009865:Oocytes / Q000502:physiology; D016366:Open Reading Frames; D011110:Polymorphism, Genetic; D011994:Recombinant Proteins / Q000378:metabolism; D012440:Saccharomyces / Q000235:genetics / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis
chemical_list: C115153:AQY1 protein, S cerevisiae; C422454:AQY2 protein, S cerevisiae; D020346:Aquaporins; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins