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J Biol Chem, Vol. 273, Issue 42, 27565-27572, October 16, 1998

Aquaporins in Saccharomyces
GENETIC AND FUNCTIONAL DISTINCTIONS BETWEEN LABORATORY AND WILD-TYPE STRAINS

From the Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species. The Saccharomyces genome data base contains an open reading frame (here designated AQY1) that encodes a protein with strong homology to aquaporins. AQY1 from laboratory and wild-type strains of Saccharomyces were expressed in Xenopus oocytes to determine the coefficients of osmotic water permeability (P_f). Oocytes injected with wild-type AQY1 cRNAs exhibit high P_f values, whereas oocytes injected with AQY1 cRNAs from laboratory strains exhibit low P_f values and have reduced levels of Aqy1p due to two amino acid substitutions. When the AQY1 gene was deleted from a wild-type yeast and cells were cultured in vitro with cycled hypo-osmolar or hyper-osmolar stresses, the AQY1 null yeast showed significantly improved viability when compared with the parental wild-type strain. We conclude that Saccharomyces cerevisiae contains at least one aquaporin gene, but it is not functional in laboratory strains due to apparent negative selection pressures resulting from in vitro methods.

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