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Protein Phosphatase Type 1 Regulates Ion Homeostasis in Saccharomyces cerevisiae
Tara Williams-Harta, Xiaolin Wua, and Kelly Tatchellaa Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71130
Corresponding author: Kelly Tatchell, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130., ktatch{at}lsuhsc.edu (E-mail)
Communicating editor: M. JOHNSTON
| ABSTRACT |
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Protein phosphatase type 1 (PP1) is encoded by the essential gene GLC7 in Saccharomyces cerevisiae. glc7-109 (K259A, R260A) has a dominant, hyperglycogen defect and a recessive, ion and drug sensitivity. Surprisingly, the hyperglycogen phenotype is partially retained in null mutants of GAC1, GIP2, and PIG1, which encode potential glycogen-targeting subunits of Glc7. The R260A substitution in GLC7 is responsible for the dominant and recessive traits of glc7-109. Another mutation at this residue, glc7-R260P, confers only salt sensitivity, indicating that the glycogen and salt traits of glc7-109 are due to defects in distinct physiological pathways. The glc7-109 mutant is sensitive to cations, aminoglycosides, and alkaline pH and exhibits increased rates of L-leucine and 3,3'-dihexyloxacarbocyanine iodide uptake, but it is resistant to molar concentrations of sorbitol or KCl, indicating that it has normal osmoregulation. KCl suppresses the ion and drug sensitivities of the glc7-109 mutant. The CsCl sensitivity of this mutant is suppressed by recessive mutations in PMA1, which encodes the essential plasma membrane H+ATPase. Together, these results indicate that Glc7 regulates ion homeostasis by controlling ion transport and/or plasma membrane potential, a new role for Glc7 in budding yeast.
PROTEIN phosphatase type 1 (PP1) is a well-characterized serine/threonine protein phosphatase (![]()
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In Saccharomyces cerevisiae, the single, essential gene GLC7 encodes PP1c and as in the case of mammalian PP1, Glc7 has been implicated in a wide range of processes based primarily on the diversity of GLC7 mutant phenotypes. GLC7 mutants have been described with defects in meiosis and sporulation (![]()
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The maintenance of ion homeostasis is an essential and highly regulated process involving numerous transport systems. These transport systems are involved in regulating cell volume, maintaining the intracellular pH and ionic composition, extracting and concentrating environmental metabolic fuels, extruding toxic substances, and generating essential ionic gradients (reviewed by ![]()
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The activity of Pma1 changes in response to extracellular glucose (![]()
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This work was motivated by the observation that glc7-109, one of 20 charged to alanine-scanning alleles, uniquely confers a NaCl-sensitive phenotype (![]()
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| MATERIALS AND METHODS |
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Yeast strains and media:
The yeast strains used in this study are listed in Table 1. All strains used in this study except KT1849 are congenic to strain KT1112 (MATa ura3-52 leu2 his3; ![]()
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Assays for ion tolerance were performed by liquid growth assays or spot dilution tests on agar media. Liquid growth assays were performed by diluting stationary phase cultures to 4 x 107 cells/ml with media described below. Cell concentrations were determined by measuring optical density at 600 nm (OD600) and/or by microscopic cell counting using a standard hemacytometer. Cultures were incubated in the specified media for 13 hr. Spot dilution tests were done by spotting three serial 10-fold dilutions of 1 x 108 cells/ml of each strain on YPD plates, synthetic media, or YPD supplemented with various concentrations of salts and drugs. Growth of strains at pH 3, 5, and 8.5 was tested in liquid YPD medium that was adjusted with 10 N KOH or 1 M HCl and buffered with 100 mM potassium phosphate or 50 mM succinate, respectively. Medium containing 0.2 mM KCl consists of a synthetic medium containing 0.5% ammonium sulfate, 2% glucose, 8 mM ammonium phosphate, 17 mM NaCl, 2 mM MgSO4, 0.2 mM CaCl2, 0.2 mM KCl, plus amino acids, vitamins, and trace elements as described (![]()
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General methods:
Escherichia coli strains DH5
F', XL1-Blue, and HB101 were used for cloning and propagation of plasmids. Diploid cells were induced to sporulate on YPA (2% potassium acetate, 2% peptone, 1% yeast extract) agar media. Yeast transformations were performed by the lithium acetate method as described (![]()
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Plasmid construction:
Plasmids used in this study are listed in Table 2. Plasmid p1407-1 is a genomic library clone in the CEN4 URA3 vector, YCp50, that contains PMA1 and a 460-bp open reading frame, YGL007. To analyze the previously described alanine-scanning allele, glc7-109 (![]()
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Isolation and characterization of glc7-109 revertants:
Three independent cultures of glc7-109 strains (KT1596 and TW25) were grown in YPD at 24° to 3 x 107 cells/ml, plated at 2 x 104 cells/ml on YPD plates containing 0.1 M CsCl, and incubated for 2 days at 24°. This concentration of CsCl completely inhibits the growth of the glc7-109 mutant. Six of 105 Cs+-tolerant revertants were characterized in detail. TW30 (pma1-s1 glc7-109), TW31 (pma1-s2 glc7-109), and TW33 (pma1-s3 glc7-109) were isolated from the first culture, TW38 (pma1-s4 glc7-109) was isolated from the second culture, and TW43 (pma1-s5glc7-109) and TW45 (pma1-s6 glc7-109) were isolated from the third culture. To assay for dominance, each revertant was mated to a glc7-109 strain and the resulting diploids were assayed for resistance to CsCl and glycogen accumulation. To determine if the reversion events were extragenic, each revertant was mated to a GLC7 strain, the resultant diploids were sporulated, and tetrad analysis was performed to assay for recovery of the glc7-109 phenotype. Linkage and complementation between the suppressors was determined by performing tetrad analysis on glc7-109 diploid strains heteroallelic for two different suppressors. On the basis of complementation and genetic linkage analysis, the six suppressors were assigned to one complementation group.
Cloning of the suppressor locus:
A pma1-s2 glc7-109 mutant strain (TW31) was transformed with a yeast genomic library in the CEN URA3 vector YCp50, and transformants were screened for growth at 37° and failure to grow on synthetic media containing 0.1 M CsCl. One transformant that was complemented for both traits was obtained from approximately 66,000 transformants. A plasmid (p1407-1) was recovered from this transformant and verified to be responsible for the complementation upon retransformation into TW31. p1407-1 was able to complement the cold sensitivity of TW60 (pma1-s1 glc7-109), TW38 (pma1-s4 glc7-109), and TW78 (pma1-s6 glc7-109). The sequence of p1407-1 was determined at the junctions between the vector and genomic insert using T7 Sequenase Version 2.0 (Amersham, Arlington Heights, IL) and primers that annealed to the YCp50 vector flanking the insert. The PMA1 gene in p1407-1 was solely responsible for complementation of the revertant phenotype, as shown by the ability of plasmid pXZ03 (a gift from James Haber), which contains only the PMA1 gene, to complement the conditional phenotypes and restore CsCl sensitivity to TW61 (pma1-s1 glc7-109), TW64 (pma1-s2 glc7-109), and TW71 (pma1-s4 glc7-109).
Genetic analysis of pma1 and calcineurin strains:
Each of the suppressor strains TW61 (pma1-s1 glc7-109), TW64 (pma1-s2 glc7-109), TW68 (pma1-s3 glc7-109), TW71 (pma1-s4 glc7-109), TW75 (pma1-s5 glc7-109), and TW79 (pma1-s6 glc7-109) were mated to strain TW82 (cnb1::LEU2) or TW83 (cnb1::LEU2). The resultant diploid strains were sporulated and the haploid segregants were assayed for conditional growth defects and growth on leu-, salt, and drug agar media described above. The mutants containing each suppressor (pma1) and calcineurin (cnb1::LEU2) were characterized.
l-Leucine uptake assays:
L-Leucine uptake assays were performed as previously described (![]()
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0.5 (5 x 106 cells/ml) at 30° in synthetic media supplemented with 0.01% leucine, histidine, and uracil. A solution of L-14C-radiolabeled leucine (11.2 GBq/mmol; CEB67, Amersham) at 304 mCi/mmol was added to the cell culture to a final concentration of 0.05 mM. At 1, 2, 3, 4, and 5 min, a 750-µl sample of cells containing L-14C-leucine was withdrawn and mixed with 750 µl ice-cold, nonlabeled 0.1 M L-leucine solution to stop uptake. The cells were immediately filtered and washed with ice-cold 0.1 M L-leucine solution as described. The L-14C-radiolabeled leucine measurements represent the average of triplicate experiments (![]()
Biochemical methods:
To assay calcineurin-dependent responsive element (CDRE)-dependent gene expression, strains were transformed with pAMS366 (![]()
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| RESULTS |
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glc7-109 mutants have a recessive, salt sensitive and a dominant, hyperglycogen phenotype:
A single GLC7 mutant (glc7-109) from a group of 20 alanine-scanning mutants was uniquely sensitive to high concentrations of NaCl (![]()
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To test the possibility that the dominant glycogen and recessive salt-sensitive phenotype of glc7-109 are independently caused by the two missense mutations in glc7-109 (K259A and R260A), we constructed mutants that contained the single missense mutations. As shown in Fig 1B, glc7-R260A confers a phenotype similar to that of glc7-109 while glc7-K259A confers a phenotype very similar to that of the wild type. Another missense mutant with proline substituted for Arg260 retains the salt and paromomycin sulfate sensitivities of R260A, but has lost the hyperglycogen phenotype. In fact, glycogen levels are reduced below that of the wild type in the glc7-R260P mutant (Fig 1B). The fact that the glc7-R260P strain retains only the salt-sensitive trait of glc7-109 supports the hypothesis that the salt-sensitive and glycogen traits are physiologically unrelated.
glc7-109 partially bypasses the requirement for the Glc7-regulatory subunits for glycogen accumulation:
The Glc7 holoenzyme that dephosphorylates and activates glycogen synthase is thought to contain Gac1, a targeting subunit that binds directly to both Glc7 and glycogen synthase (![]()
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The yeast genome contains three additional genes whose products are similar to Gac1. PIG1, PIG2, and GIP2 were identified in a two-hybrid screen for Gsy2-interaction proteins (![]()
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Glc7 and calcineurin act through different pathways to affect ion homeostasis:
Yeast strains lacking the ser/thr protein phosphatase calcineurin/PP2B are sensitive to high concentrations of Na+, Li+, and Mn2+ (![]()
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The apparent similarity between the calcineurin and glc7-109 phenotypes prompted us to directly compare the two mutants. We used a cnb1::LEU2 null mutant for the comparison. CNB1 encodes a conserved regulatory subunit of calcineurin (![]()
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The glc7-109 strain exhibits increased rates of l-leucine uptake:
The glc7-109 mutant is hypersensitive to the aminoglycoside antibiotics paromomycin sulfate and hygromycin B. Since the mechanisms of action of these two antibiotics are different, it is likely that the hypersensitivity of glc7-109 strains to these drugs is caused by defects in uptake or export. Although we have not been able to distinguish between these two possibilities, we note that glc7-109 strains grow more rapidly than the wild type on synthetic media containing low concentrations of amino acids (data not shown). To confirm that this difference is due to a change in amino acid uptake we measured L-leucine uptake in glc7-109 mutants The rate of L-leucine uptake in the glc7-109 mutant was approximately twofold higher than that in the wild type (Table 3).
Many defects due to glc7-109 are K+ remedial:
To rule out the possibility that the sensitivity of glc7-109 mutants to high concentrations of ions was due to osmotic effects, we tested the growth properties of glc7-109 strains on YPD media containing 1 M KCl and 1 M sorbitol. While no growth defects were observed on media with only KCl or sorbitol, KCl partially relieved the salt and drug sensitivities of glc7-109 strains. The presence of 200 mM KCl in the medium reduces the sensitivity of glc7-109 to Cs+, Li+, hygromycin B, and paromomycin sulfate (Fig 5), and to Mn2+ and Na+ (data not shown). The K+ remedial phenotype caused by glc7-109 led us to examine its effect on growth on low concentrations of KCl, because mutants defective in the potassium transporters Trk1 and Trk2 are hypersensitive to hygromycin B and toxic cations (![]()
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Suppressors of the Cs+-sensitive phenotype of glc7-109:
We characterized six spontaneous glc7-109 revertants that grew on YPD medium containing 0.1 M CsCl, as described in MATERIALS AND METHODS. The mutations responsible for the reversion events were recessive, as shown by CsCl sensitivity of diploid strains heterozygous for suppressor mutations and homozygous for glc7-109. To determine if the mutations responsible for suppression were extragenic to GLC7, tetrad analysis was performed on diploid strains created by mating each of the six revertants to a wild-type strain. The salt-sensitive phenotype of glc7-109 was observed in approximately one-fourth of the spore clones from each cross, indicating that the mutation responsible for the reversion was unlinked to GLC7. To determine if the suppressors were in the same complementation group, diploid strains were constructed that were homozygous for glc7-109 and heterozygous for two different suppressors. All diploids were resistant to 0.1 M CsCl, indicating that all suppressors were in the same complementation group. Furthermore, tetrad analysis of meiotic progeny of these diploid strains revealed that all spore clones retained the Cs+-resistant phenotype of the parents, indicating that the suppressor loci are tightly linked.
Although these suppressors are genetically linked, they confer diverse phenotypes. While all six revertants are able to grow on media containing 0.1 M CsCl or 0.9 M NaCl, only pma1-s1, pma1-s3, and pma1-s4 suppress the Li+ defect of glc7-109 (Fig 6). In contrast, pma1-s1 and pma1-s4 strains actually grow better than the wild-type strain on 0.1 M LiCl (Fig 6). No revertant strains except those containing pma1-s2 exhibit the glc7-109 growth defect on 10 mM MnCl2 (Fig 6). Some of these revertants also have conditional growth defects in the glc7-109 genetic background. pma1-s2 and pma1-s5 strains grow more slowly than the wild-type strain at 37° while pma1-s1, pma1-s4, and pma1-s6 strains grow more slowly than the wild type at 15° (Fig 6). These six suppressor mutants were also characterized in a wild-type GLC7 background. pma1-s6 strains grow poorly on 0.1 M CsCl and 0.1 M LiCl, whereas pma1-s2 grows poorly on LiCl (Fig 7). In contrast, the pma1-s1, pma1-s3, pma1-s4, and pma1-s5 strains grow faster than the wild-type strain on LiCl (Fig 7). Most of the conditional growth defects observed in a glc7-109 background were also apparent in a GLC7+ background. For example, pma1-s1 and pma1-s4 strains grow more slowly than the wild type at 15° (Fig 7) and pma1-s2 strains grow more slowly than the wild type at 37° (data not shown).
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The glc7-109 suppressors are allelic to PMA1, encoding the essential plasma membrane H+ATPase:
The suppressor locus was cloned by complementation of the temperature sensitivity of strain TW64 (pma1-s2 glc7-109) as described in MATERIALS AND METHODS. The complementing plasmid clone (p1407-1) also complemented the cold-sensitive defects of strains TW30 (pma1-s1 glc7-109) and TW38 (pma1-s4 glc7-109). These transformants grew well at 37° and 15°, but failed to grow on 0.1 M CsCl media. Sequence analysis revealed that the genomic insert in p1407-1 contained PMA1 and an adjacent 378-bp open reading frame, YGL007. A plasmid (pXZ03) containing PMA1 but lacking YGL007 was also able to suppress the temperature sensitivity and Cs+ resistance of TW64 (pma1-s2 glc7-109), indicating that PMA1 is responsible for the complementation. To confirm that the suppressor mutations are alleles of PMA1, we mapped the distance between pma1-s4 and leu1, which lies
1 cM centromere proximal to PMA1. Tetrad analysis of a cross between KT1850 (MAT
ura3-52 his3 glc7-109 pma1-s4) and KT1849 (MATa ura3-52 his3 leu1) revealed that the distance between leu1 and pma1-s4 is 1.1 cM (P:NP:T = 43:0:1), identical to the previously determined map distance (P:NP:T = 869:0:22; ![]()
PMA1 mutants have been isolated that suppress the salt sensitivities of calcineurin mutants (![]()
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Many pma1 mutants are sensitive to low pH (![]()
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The ability of pma1 mutations to suppress the salt-sensitive phenotype of glc7-109 led us to assay Pma1 levels and activity in glc7-109 and pma1-s4 mutants. Pma1 levels in the glc7-109 strain were
90% that of the wild type, as assayed by immunoblot analysis. Vanadate-sensitive ATPase activities, a measure of Pma1 activity, were comparable in the wild-type and glc7-109 strains (Table 3), but that of the pma1-s4 mutant is 61% that of the wild type (data not shown). Indirect immunofluorescence revealed no obvious differences between glc7-109 and wild-type strains in Pma1 localization (data not shown). Thus, we find no compelling evidence that glc7-109 directly influences the activity, abundance, or distribution of Pma1.
glc7-109 cells may be hyperpolarized:
The potassium-remedial sensitivity of glc7-109 mutants to toxic cations, high pH, and aminoglycoside antibiotics and the suppression of these defects by mutations in PMA1 are consistent with the hypothesis that the plasma membrane potential of the glc7-109 mutant is hyperpolarized. A conventional determination of membrane potential using electrophysiological methods is not possible in yeast, but relative membrane potentials can be assessed using fluorescent dyes. Although such methods suffer from complications caused by the contribution of the mitochondria to the uptake process, ![]()
150200% that of the wild-type strain. In contrast, DiOC6(3) fluorescence in a pma1-s4 strain, TW72, was only 3040% that of wild type and that of the pma1-s4 glc7-109 strain (TW71) was only 5060% of wild type. As a control, we assayed DiOC6(3) fluorescence in a wild-type strain grown in synthetic media containing a low concentration of K+, which is known to hyperpolarize the plasma membrane (![]()
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| DISCUSSION |
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Like many glc7 mutations, glc7-109 is very pleiotropic. The glc7-109 mutant hyperaccumulates glycogen and is sensitive to a wide range of cations, high pH, and aminoglycoside antibiotics. The analysis of the single missense mutations that make up glc7-109 indicated that the R260A substitution is responsible for all the traits conferred by glc7-109. It is likely that the hyperglycogen trait and the ion and drug hypersensitivity traits reflect the influence of Glc7 on at least two separate physiological processes. This is because the glycogen phenotype of glc7-109 is dominant, whereas the other traits are recessive, and because glc7-R260P confers the ion-related defects but not the hyperglycogen phenotype. Yeast PP1 has been associated with glycogen metabolism for years; its acronym was derived from the glycogen deficiency of glc7-1 (![]()
glc7-109 and glycogen:
In yeast, as in mammals, PP1 is thought to dephosphorylate and activate glycogen synthase. PP1 activity toward glycogen synthase is thought to be regulated by targeting subunits that tether PP1c to glycogen synthase. Abundant evidence indicates that Gac1 plays this role in yeast. gac1 null mutants accumulate low levels of glycogen and glycogen synthase in these strains remains in a phosphorylated, inactive form (![]()
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One explanation for these results is that additional glycogen-targeting subunits can substitute for the loss of Gac1, Pig1, and Gip2. Pig2 is a candidate for such a redundant subunit. It is most similar in sequence to Gip2 and although loss-of-function mutations in PIG2 have not been found to alter glycogen levels, it is possible that Glc7-109 could recruit Pig2 in the absence of other targeting subunits. Another possibility is that the high levels of glycogen in glc7-109 strains are partially due to changes in the activity of enzymes other than glycogen synthase. We have not assayed activity levels of glycogen synthase in our strains and we cannot rule out the possibility that the degradative pathway is altered in glc7-109 strains. It is worth noting that Pho85, the kinase that phosphorylates glycogen synthase, also regulates the activity of glycogen phosphorylase through cyclins Pcl6 and Pcl7 (![]()
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Glc7 and ion homeostasis:
The pleiotropic salt- and drug-sensitive phenotype conferred by glc7-109 can be accounted for by at least two broad mechanisms. One possible explanation is that the glc7-109 mutant has a hyperpolarized plasma membrane potential. In Neurospora crassa, in which membrane voltage measurements can be performed (![]()
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How could Glc7 act to influence membrane potential? The two most obvious possibilities are via Pma1 and the potassium transporters, Trk1 and Trk2. Pma1 is essential for maintenance of the plasma membrane potential and its activity is regulated in response to a range of external factors. Pma1 is phosphorylated at multiple sites and at least two classes of protein kinases may regulate its activity (![]()
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The potassium transporters Trk1 and Trk2 are also candidates for Glc7 regulation. Like glc7-109, trk1 and trk1 trk2 double mutants exhibit high levels of DiOC6(3) fluorescence (![]()
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An alternative explanation to hyperpolarization for the pleiotropic drug- and ion-hypersensitive phenotype of the glc7-109 mutant is that glc7-109 results in the activation of a nonspecific uptake mechanism or conductance. In this scenario, a reduction of Pma1 activity or the application of exogenous K+ could suppress the drug and ion toxicity of the glc7-109 mutation through indirect effects. In this regard, we note that ![]()
| ACKNOWLEDGMENTS |
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We thank Carolyn Slayman and Ken Allen for providing antibody to Pma1 and for helpful advice concerning Pma1 activity assays. We acknowledge Martha Cyert, James Haber, and Peter Roach for kindly providing strains and plasmids. We thank Andrew Bloecher, Lucy Robinson, Heather Panek, Clifford Slayman, and Guglielmo M. Venturi for helpful discussions. We gratefully acknowledge Clifford Slayman and Lucy Robinson for critically reading this manuscript. This work was funded by National Institutes of Health research grant GM-47789.
Manuscript received September 18, 2001; Accepted for publication January 25, 2002.
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