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Yeast Fex1p Is a Constitutively Expressed Fluoride Channel with Functional Asymmetry of Its Two Homologous Domains

Smith, Kathryn D., Gordon, Patricia B., Rivetta, Alberto, Allen, Kenneth E., Berbasova, Tetyana, Slayman, Clifford, Strobel, Scott A.·2015·Journal of Biological Chemistry
DOI 10.1074/jbc.m115.651976
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FIGURE 1 Both yeast FEX proteins conduct channel-like currents in the presence of cytoplasmic fluoride. A, currents measured via whole-cell patch clamping on representative yeast spheroplasts from four different strains as follows: WT for both FEX genes ( left column, top panel ); knock-out of both FEX genes ( right column, top panel ); knock-out of FEX2 ( left column, middle panel ); and knock-out of FEX1 ( right column, middle panel ). The standard condition used 75 mM potassium fluoride in the pipette (cytoplasmic) solution and that yielded maximal steady-state currents between -48 and -86 mV for both single knock-out strains and between -78 and -143 pA in WT cells examined (at -180mV).Residualcurrent under the same conditions but absent in both FEX genes/proteins was ∼ 5%; residual current with full salt replacement by KCl was ∼ 15%. Recorded traces were not corrected for leakagecurrents. Currents for typical scans are shown as stacked 1.5-s traces, with negative (downward) currents designating cation flux from the bath to the cell interior. Heavy traces continued to the left and right of each stack represent clamp current at the holding voltage of -40 mV; dotted lines designate thecurrentforzerovoltage. B, plot of averaged currents for 6-8 separate cells for each strain, similar to those in A , versus clampedmembranevoltage.Averages were calculated over the last 500 ms of each trace, pre-corrected for leakage currents (29). Error bars designate 1 S.E. pH i = 7.0 in all cases, and salt for osmotic balance was potassium gluconate. External solution, Buffer D, pH 7.5 (see experimental procedures). All four yeast strains carried a deletion of the PMR1 gene ( pmr1 𝚫 ) a Golgi-resident calcium pump (30), which produces enlarged cells for easy patch clamping. Very small apparent positive currents at low voltages are a leakage artifact.
FIGURE 1 Both yeast FEX proteins conduct channel-like currents in the presence of cytoplasmic fluoride. A, currents measured via whole-cell patch clamping on representative yeast spheroplasts from four different strains as follows: WT for both FEX genes ( left column, top panel ); knock-out of both FEX genes ( right column, top panel ); knock-out of FEX2 ( left column, middle panel ); and knock-out of FEX1 ( right column, middle panel ). The standard condition used 75 mM potassium fluoride in the pipette (cytoplasmic) solution and that yielded maximal steady-state currents between -48 and -86 mV for both single knock-out strains and between -78 and -143 pA in WT cells examined (at -180mV).Residualcurrent under the same conditions but absent in both FEX genes/proteins was ∼ 5%; residual current with full salt replacement by KCl was ∼ 15%. Recorded traces were not corrected for leakagecurrents. Currents for typical scans are shown as stacked 1.5-s traces, with negative (downward) currents designating cation flux from the bath to the cell interior. Heavy traces continued to the left and right of each stack represent clamp current at the holding voltage of -40 mV; dotted lines designate thecurrentforzerovoltage. B, plot of averaged currents for 6-8 separate cells for each strain, similar to those in A , versus clampedmembranevoltage.Averages were calculated over the last 500 ms of each trace, pre-corrected for leakage currents (29). Error bars designate 1 S.E. pH i = 7.0 in all cases, and salt for osmotic balance was potassium gluconate. External solution, Buffer D, pH 7.5 (see experimental procedures). All four yeast strains carried a deletion of the PMR1 gene ( pmr1 𝚫 ) a Golgi-resident calcium pump (30), which produces enlarged cells for easy patch clamping. Very small apparent positive currents at low voltages are a leakage artifact.CC-BY · From the PDF
FIGURE 2 Quantification of FEX proteins in yeast plasma membranes. Lower inset, Western blot of HA-tagged Fex1p and Fex2p. Each band represents 4 𝛍 gofmembraneprotein. 1a and 1b are samples from FEX1-HA; 2a and 2b are samples from 𝚫 fex1 FEX2-HA; and 1,2a and 1,2b are samples from FEX1-HA FEX2-HA. Upper inset, Western blot of HA-tagged Saccharomyces Pma1p (calibrating standard) in known ratio (20%) to the partially purified membrane protein. 2-5 ng of the standards contained 4, 6, 8, and 10 fmol of Pma1p-HA, respectively, for the four plotted red points . The (least squares) parabola = -1.18 X 2 + 6.54 X + 2.02, fitted to the red points, was used for direct calculation of femtomoles of HA associated with each protein sample of Fex1p or Fex2p. a.u., arbitrary units.
FIGURE 2 Quantification of FEX proteins in yeast plasma membranes. Lower inset, Western blot of HA-tagged Fex1p and Fex2p. Each band represents 4 𝛍 gofmembraneprotein. 1a and 1b are samples from FEX1-HA; 2a and 2b are samples from 𝚫 fex1 FEX2-HA; and 1,2a and 1,2b are samples from FEX1-HA FEX2-HA. Upper inset, Western blot of HA-tagged Saccharomyces Pma1p (calibrating standard) in known ratio (20%) to the partially purified membrane protein. 2-5 ng of the standards contained 4, 6, 8, and 10 fmol of Pma1p-HA, respectively, for the four plotted red points . The (least squares) parabola = -1.18 X 2 + 6.54 X + 2.02, fitted to the red points, was used for direct calculation of femtomoles of HA associated with each protein sample of Fex1p or Fex2p. a.u., arbitrary units.CC-BY · From the PDF
Image 3
CC-BY · From the PDF
FIGURE 3 FEX-mediated currents vary with cytoplasmic fluoride concentration. A, representative traces of whole-cell currents from different spheroplasts, for experiments similar to that in Fig. 1 A but with differing [F -] i in the patch pipette. B, current-voltage relationships averaged for the full set of experiments. Plot of pA versus [F -] i at -180mVfitsaMichaelis curve with K 0.5 ∼ 64 mM. Yeast strain is as follows: FEX1 FEX2 pmr1 𝚫 . [Cl -] i was kept at 8 mM throughout, and osmotic balance was maintained by potassium gluconate. Error bars are S.E. values for n = 7, 5, 6, 8, 3, and 1 trials on different cells, with [F -] i = 75, 37.5, …, 4.7, and 0 mM, respectively.
FIGURE 3 FEX-mediated currents vary with cytoplasmic fluoride concentration. A, representative traces of whole-cell currents from different spheroplasts, for experiments similar to that in Fig. 1 A but with differing [F -] i in the patch pipette. B, current-voltage relationships averaged for the full set of experiments. Plot of pA versus [F -] i at -180mVfitsaMichaelis curve with K 0.5 ∼ 64 mM. Yeast strain is as follows: FEX1 FEX2 pmr1 𝚫 . [Cl -] i was kept at 8 mM throughout, and osmotic balance was maintained by potassium gluconate. Error bars are S.E. values for n = 7, 5, 6, 8, 3, and 1 trials on different cells, with [F -] i = 75, 37.5, …, 4.7, and 0 mM, respectively.CC-BY · From the PDF
FIGURE 4 Fex1p is localized at the yeast plasma membrane. A, growth of GFP-tagged FEX1 strains on several concentrations of NaF. B, images of yeast strains with and without GFP-tagged FEX1. White arrows show examples of punctate GFP expression. Images of WT, N-GFP-FEX1, and FEX1-165-GFP were taken with a 3-s exposure for fluorescence and a 150-ms exposure for differential interference contrast ( DIC ). Overexpression was imaged by a 500-ms exposure for fluorescence.
FIGURE 4 Fex1p is localized at the yeast plasma membrane. A, growth of GFP-tagged FEX1 strains on several concentrations of NaF. B, images of yeast strains with and without GFP-tagged FEX1. White arrows show examples of punctate GFP expression. Images of WT, N-GFP-FEX1, and FEX1-165-GFP were taken with a 3-s exposure for fluorescence and a 150-ms exposure for differential interference contrast ( DIC ). Overexpression was imaged by a 500-ms exposure for fluorescence.CC-BY · From the PDF
FIGURE 5 FEX is constitutively expressed in actively growing yeast. A, Northern blot showing mRNA levels of FEX1 and FEX2 as a function of time of exposuretoNaF. B, Westernblotshowingthecorrespondingproteinlevelsof FEX1. C, demonstration that localization of Fex1p does not change in the presence/absence of fluoride. Images taken using a 5-s exposure for fluorescence and 150-ms exposure for differential interference contrast ( DIC ).
FIGURE 5 FEX is constitutively expressed in actively growing yeast. A, Northern blot showing mRNA levels of FEX1 and FEX2 as a function of time of exposuretoNaF. B, Westernblotshowingthecorrespondingproteinlevelsof FEX1. C, demonstration that localization of Fex1p does not change in the presence/absence of fluoride. Images taken using a 5-s exposure for fluorescence and 150-ms exposure for differential interference contrast ( DIC ).CC-BY · From the PDF
FIGURE 6 FEX1 and FEX2 are expressed at visually equivalent levels. Fluorescent imaging of strains with both Fex1p and Fex2p labeled is shown. Arrows showrepresentative examples of GFP and mCherry fluorescence. DIC, differential interference contrast.
FIGURE 6 FEX1 and FEX2 are expressed at visually equivalent levels. Fluorescent imaging of strains with both Fex1p and Fex2p labeled is shown. Arrows showrepresentative examples of GFP and mCherry fluorescence. DIC, differential interference contrast.CC-BY · From the PDF
FIGURE 7 Fex1pis folded as an antiparallel dimer. A, topology model as predicted by the PHOBIUS (43) and TMHMM (42) programs. B, images of five strains expressing gGFP-tagged FEX1. The absence of fluorescence implies that the GFP tag is extracellular; the presence of fluorescence implies that the tag is intracellular. All images were taken with a 500-ms exposure for fluorescence and a 150-ms exposure for differential interference contrast ( DIC ).
FIGURE 7 Fex1pis folded as an antiparallel dimer. A, topology model as predicted by the PHOBIUS (43) and TMHMM (42) programs. B, images of five strains expressing gGFP-tagged FEX1. The absence of fluorescence implies that the GFP tag is extracellular; the presence of fluorescence implies that the tag is intracellular. All images were taken with a 500-ms exposure for fluorescence and a 150-ms exposure for differential interference contrast ( DIC ).CC-BY · From the PDF
Image 9
CC-BY · From the PDF
FIGURE8 Dom1andDom2arenotfunctionalindividually,butFlucisactiveinyeast. A, Dom1,Dom2,andFlucfrom E. coli . The N- and C-terminal elements highlightedin red wereclonedfrom FEX1 toprovidenativetermini. B, fex1 𝚫 fex2 𝚫 yeastexpressingeachconstructfrom A weregrownonYPDmediacontaining 5 mM NaF.
FIGURE8 Dom1andDom2arenotfunctionalindividually,butFlucisactiveinyeast. A, Dom1,Dom2,andFlucfrom E. coli . The N- and C-terminal elements highlightedin red wereclonedfrom FEX1 toprovidenativetermini. B, fex1 𝚫 fex2 𝚫 yeastexpressingeachconstructfrom A weregrownonYPDmediacontaining 5 mM NaF.CC-BY · From the PDF
FIGURE9 Residue conservation between Fex1p and some of its homologs. A, alignment of Fex1p, one archaeal sequence, and two eubacterial sequences. Theeukaryotic consensus sequences for Dom1 and Dom2 as generated by PROMALS3D (46) are shown below the alignment. The most conserved amino acids are highlighted in red . h = hydrophobic (W, F, Y, M, L, I, V, A, C, T, H); s = small (A, G, C, S, V, N, D, T, P); t = tiny (A, G, C, S); l = aliphatic (I, V, L); @ = aromatic (Y, H, W, F); o = alcohol (S, T). B, bead diagram of Fex1p, elaborated from the topology model in Fig. 7 A . Conserved residues targeted for mutagenesis are highlighted in red . Boundaries for the TMHs were predicted by TMHMM with the exception of the C-terminal end of TM1. The predicted boundary of this helix does not place Arg-33 within the membrane. However, the conserved nature of this residue, the prediction for Arg-255 in TM1 ′ , and the transmembrane location of the analogous Arg in prokaryotic homologs suggests that Arg-33 likely resides in TM1, and it has been modeled as such.
FIGURE9 Residue conservation between Fex1p and some of its homologs. A, alignment of Fex1p, one archaeal sequence, and two eubacterial sequences. Theeukaryotic consensus sequences for Dom1 and Dom2 as generated by PROMALS3D (46) are shown below the alignment. The most conserved amino acids are highlighted in red . h = hydrophobic (W, F, Y, M, L, I, V, A, C, T, H); s = small (A, G, C, S, V, N, D, T, P); t = tiny (A, G, C, S); l = aliphatic (I, V, L); @ = aromatic (Y, H, W, F); o = alcohol (S, T). B, bead diagram of Fex1p, elaborated from the topology model in Fig. 7 A . Conserved residues targeted for mutagenesis are highlighted in red . Boundaries for the TMHs were predicted by TMHMM with the exception of the C-terminal end of TM1. The predicted boundary of this helix does not place Arg-33 within the membrane. However, the conserved nature of this residue, the prediction for Arg-255 in TM1 ′ , and the transmembrane location of the analogous Arg in prokaryotic homologs suggests that Arg-33 likely resides in TM1, and it has been modeled as such.CC-BY · From the PDF
FIGURE 10 Growth tolerance plots of point mutants of Fex1p. Relative AUCis the area under the curve normalized to the growth at zero fluoride. The data are fitted to a standard dose-response curve, where each curve wasmeasuredaminimumofthreetimes. Error bars represent the standard deviation. Wild-type pRS416FEX1 ( f ) and empty pRS416 ( F ) are shown on each graph for reference. IC 50 values calculated from these curves are shown in Table 4. A, mutations to domain 1: G29A ( , ), R33A ( H12135 ), 32insA ( c141 ), N56A ( ✷ ), and S97A ( E ). B, mutations to domain 2: A251G ( , ), R255A ( H12135 ), 254insA ( c141 ), N277A ( ✷ ), and S328A ( E ). C, mutations to both domain 1 and 2: G29A/A251G ( , ), R33A/R255A ( H12135 ), 32insA/245insA ( c141 ), N56A/ N277A ( ✷ ), and S97A/S328A ( E ).
FIGURE 10 Growth tolerance plots of point mutants of Fex1p. Relative AUCis the area under the curve normalized to the growth at zero fluoride. The data are fitted to a standard dose-response curve, where each curve wasmeasuredaminimumofthreetimes. Error bars represent the standard deviation. Wild-type pRS416FEX1 ( f ) and empty pRS416 ( F ) are shown on each graph for reference. IC 50 values calculated from these curves are shown in Table 4. A, mutations to domain 1: G29A ( , ), R33A ( H12135 ), 32insA ( c141 ), N56A ( ✷ ), and S97A ( E ). B, mutations to domain 2: A251G ( , ), R255A ( H12135 ), 254insA ( c141 ), N277A ( ✷ ), and S328A ( E ). C, mutations to both domain 1 and 2: G29A/A251G ( , ), R33A/R255A ( H12135 ), 32insA/245insA ( c141 ), N56A/ N277A ( ✷ ), and S97A/S328A ( E ).CC-BY · From the PDF
FIGURE11 Relative IC 50 values for mutants of Arg-33 and Arg-255 in TM1 ( A ) and Asn-56 and Asn-277 in TM2 ( B ). To calculate the relative IC 50 , the point mutant IC 50 from Table 4 was divided by the IC 50 value for wild type. D1 = mutation in domain 1; D2 = mutation in domain 2; D1/2 = mutation in both domain 1 and domain 2.
FIGURE11 Relative IC 50 values for mutants of Arg-33 and Arg-255 in TM1 ( A ) and Asn-56 and Asn-277 in TM2 ( B ). To calculate the relative IC 50 , the point mutant IC 50 from Table 4 was divided by the IC 50 value for wild type. D1 = mutation in domain 1; D2 = mutation in domain 2; D1/2 = mutation in both domain 1 and domain 2.CC-BY · From the PDF

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Metadata

Authors
Smith, K. D., Gordon, P. B., Rivetta, A., Allen, K. E., Berbasova, T., Slayman, C., & Strobel, S. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2015-08
Volume
290
Issue
32
Pages
19874-19887
ISSN
0021-9258
DOI
10.1074/jbc.m115.651976
Cited by
41
References
3
Language
en
Licence
Funders
National Institutes of Health (GM60696, GM022778)

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