TY - JOUR
T1 - The Schizosaccharomyces pombe Pzh1 protein phosphatase regulates Na+ ion influx in a Trk1-independent fashion
AU - Balcells, Lluís
AU - Calero, Fernando
AU - Gómez, Néstor
AU - Ramos, José
AU - Ariño, Joaquín
PY - 1999/2/15
Y1 - 1999/2/15
N2 - We have previously shown that fission yeast encodes a PPZ-like phosphatase, designated Pzh1, which is an important determinant of cation homeostasis. pzh1Δ mutants display increased tolerance to Na+ ions, but they are hypersensitive to KCl [Balcells, L., Gomez, N., Casamayor, A., Clotet, J. and Arino, J. (1997) Eur. J. Biochem. 250, 476-483]. We have immunodetected Pzh1 in yeast extracts and found that this phosphatase is largely associated with particulate fractions. Cells defective in Pzh1 do not show altered efflux of Na+ or Li+ ions, but they accumulate these cations more slowly than wild-type cells. K+ ion content of pzh1Δ cells is about twice that of wild-type cells, and this can be explained by decreased efflux of K+. Therefore, Pzh1 may regulate both Na+ influx and K+ efflux in fission yeast. To test the possible relationship between K+ uptake, Na+ tolerance and Pzh1 function, we deleted the trk1+ gene, which encodes a putative high-affinity transporter of K+ ions. trk1Δ mutants grew well even at relatively low concentrations of KCl and did not show significantly altered content or influx of K+ ions. However, they showed a Na+-sensitive phenotype which was greatly intensified by deletion of the sod2+ gene (which encodes the major determinant for efflux of Na+ ions), and clearly ameliorated by deletion of the pzh1 phosphatase, as well as by moderate concentrations of KCl in the medium. These results suggest that Trk1 does not mediate the effect of Pzh1 on NaCl tolerance and that fission yeast contains efficient systems, other than Trk1, for uptake of K+ ions.
AB - We have previously shown that fission yeast encodes a PPZ-like phosphatase, designated Pzh1, which is an important determinant of cation homeostasis. pzh1Δ mutants display increased tolerance to Na+ ions, but they are hypersensitive to KCl [Balcells, L., Gomez, N., Casamayor, A., Clotet, J. and Arino, J. (1997) Eur. J. Biochem. 250, 476-483]. We have immunodetected Pzh1 in yeast extracts and found that this phosphatase is largely associated with particulate fractions. Cells defective in Pzh1 do not show altered efflux of Na+ or Li+ ions, but they accumulate these cations more slowly than wild-type cells. K+ ion content of pzh1Δ cells is about twice that of wild-type cells, and this can be explained by decreased efflux of K+. Therefore, Pzh1 may regulate both Na+ influx and K+ efflux in fission yeast. To test the possible relationship between K+ uptake, Na+ tolerance and Pzh1 function, we deleted the trk1+ gene, which encodes a putative high-affinity transporter of K+ ions. trk1Δ mutants grew well even at relatively low concentrations of KCl and did not show significantly altered content or influx of K+ ions. However, they showed a Na+-sensitive phenotype which was greatly intensified by deletion of the sod2+ gene (which encodes the major determinant for efflux of Na+ ions), and clearly ameliorated by deletion of the pzh1 phosphatase, as well as by moderate concentrations of KCl in the medium. These results suggest that Trk1 does not mediate the effect of Pzh1 on NaCl tolerance and that fission yeast contains efficient systems, other than Trk1, for uptake of K+ ions.
KW - Cation fluxes
KW - Fission yeast
KW - Protein phosphatase
KW - Salt tolerance
U2 - 10.1046/j.1432-1327.1999.00129.x
DO - 10.1046/j.1432-1327.1999.00129.x
M3 - Article
SN - 0014-2956
VL - 260
SP - 31
EP - 37
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
ER -