Aquaporins in Saccharomyces: Characterization of a second functional water channel protein

Jennifer M. Carbrey, Mélanie Bonhivers, Jef D. Boeke, Peter Agre

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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 ∑1278b. AQY2 is disrupted by a stop codon in most strains; however, ∑1278b has an intact ORF. Because ∑1278b 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 ∑1278b Aqy2p (Pro-141). S. chevalieri Aqy2p is a functional water channel in oocytes and traffics to the plasma membrane of yeast. The ∑1278b 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, ∑1278b 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.

Original languageEnglish (US)
Pages (from-to)1000-1005
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number3
DOIs
StatePublished - Jan 30 2001

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