Characterization of the Pho89 phosphate transporter by functional hyperexpression in Saccharomyces cerevisiae
Abstract The Na+-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Δ pho87Δ pho90Δ pho91Δ quadruple deletion strain of S. cerevisiae...
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| Veröffentlicht in: | FEMS yeast research Jg. 8; H. 5; S. 685 - 696 |
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| Format: | Journal Article |
| Sprache: | Englisch |
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Oxford, UK
Blackwell Publishing Ltd
01.08.2008
Oxford University Press |
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| ISSN: | 1567-1356, 1567-1364, 1567-1364 |
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| Abstract | Abstract
The Na+-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Δ pho87Δ pho90Δ pho91Δ quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high-capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5–8.0, the transporter is functionally active under alkaline conditions only, with a Km value reflecting high-affinity properties of the transporter and with a transport rate about 100-fold higher than that of the protein in a wild-type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89-mediated phosphate uptake at alkaline pH is cation-dependent with a strong activation by Na+ ions and sensitivity to carbonyl cyanide m-chlorophenylhydrazone. The contribution of H+- and Na+-coupled phosphate transport systems in wild-type cells grown at different pH values was quantified. The contribution of the Na+-coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH. |
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| AbstractList | The Na+‐coupled, high‐affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Δpho87Δpho90Δpho91Δ quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high‐capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5–8.0, the transporter is functionally active under alkaline conditions only, with a Km value reflecting high‐affinity properties of the transporter and with a transport rate about 100‐fold higher than that of the protein in a wild‐type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89‐mediated phosphate uptake at alkaline pH is cation‐dependent with a strong activation by Na+ ions and sensitivity to carbonyl cyanide m‐chlorophenylhydrazone. The contribution of H+‐ and Na+‐coupled phosphate transport systems in wild‐type cells grown at different pH values was quantified. The contribution of the Na+‐coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH. The Na(+)-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Deltapho87Deltapho90Deltapho91Delta quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high-capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5-8.0, the transporter is functionally active under alkaline conditions only, with a K(m) value reflecting high-affinity properties of the transporter and with a transport rate about 100-fold higher than that of the protein in a wild-type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89-mediated phosphate uptake at alkaline pH is cation-dependent with a strong activation by Na(+) ions and sensitivity to carbonyl cyanide m-chlorophenylhydrazone. The contribution of H(+)- and Na(+)-coupled phosphate transport systems in wild-type cells grown at different pH values was quantified. The contribution of the Na(+)-coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH.The Na(+)-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Deltapho87Deltapho90Deltapho91Delta quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high-capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5-8.0, the transporter is functionally active under alkaline conditions only, with a K(m) value reflecting high-affinity properties of the transporter and with a transport rate about 100-fold higher than that of the protein in a wild-type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89-mediated phosphate uptake at alkaline pH is cation-dependent with a strong activation by Na(+) ions and sensitivity to carbonyl cyanide m-chlorophenylhydrazone. The contribution of H(+)- and Na(+)-coupled phosphate transport systems in wild-type cells grown at different pH values was quantified. The contribution of the Na(+)-coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH. The Na+-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Δ pho87Δ pho90Δ pho91Δ quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high-capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5–8.0, the transporter is functionally active under alkaline conditions only, with a Km value reflecting high-affinity properties of the transporter and with a transport rate about 100-fold higher than that of the protein in a wild-type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89-mediated phosphate uptake at alkaline pH is cation-dependent with a strong activation by Na+ ions and sensitivity to carbonyl cyanide m-chlorophenylhydrazone. The contribution of H+- and Na+-coupled phosphate transport systems in wild-type cells grown at different pH values was quantified. The contribution of the Na+-coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH. The Na⁺-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Δpho87Δpho90Δpho91Δ quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high-capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5-8.0, the transporter is functionally active under alkaline conditions only, with a Km value reflecting high-affinity properties of the transporter and with a transport rate about 100-fold higher than that of the protein in a wild-type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89-mediated phosphate uptake at alkaline pH is cation-dependent with a strong activation by Na⁺ ions and sensitivity to carbonyl cyanide m-chlorophenylhydrazone. The contribution of H⁺- and Na⁺-coupled phosphate transport systems in wild-type cells grown at different pH values was quantified. The contribution of the Na⁺-coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH. Abstract The Na+-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Δ pho87Δ pho90Δ pho91Δ quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high-capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5–8.0, the transporter is functionally active under alkaline conditions only, with a Km value reflecting high-affinity properties of the transporter and with a transport rate about 100-fold higher than that of the protein in a wild-type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89-mediated phosphate uptake at alkaline pH is cation-dependent with a strong activation by Na+ ions and sensitivity to carbonyl cyanide m-chlorophenylhydrazone. The contribution of H+- and Na+-coupled phosphate transport systems in wild-type cells grown at different pH values was quantified. The contribution of the Na+-coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH. The Na(+)-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low activity and special properties. In this study, we have used a pho84Deltapho87Deltapho90Deltapho91Delta quadruple deletion strain of S. cerevisiae devoid of all transporter genes specific for inorganic phosphate, except for PHO89, to functionally characterize Pho89 under conditions where its expression is hyperstimulated. Under these conditions, the Pho89 protein is strongly upregulated and is the sole high-capacity phosphate transporter sustaining cellular acquisition of inorganic phosphate. Even if Pho89 is synthesized in cells grown at pH 4.5-8.0, the transporter is functionally active under alkaline conditions only, with a K(m) value reflecting high-affinity properties of the transporter and with a transport rate about 100-fold higher than that of the protein in a wild-type strain. Even under these hyperexpressive conditions, Pho89 is unable to sense and signal extracellular phosphate levels. In cells grown at pH 8.0, Pho89-mediated phosphate uptake at alkaline pH is cation-dependent with a strong activation by Na(+) ions and sensitivity to carbonyl cyanide m-chlorophenylhydrazone. The contribution of H(+)- and Na(+)-coupled phosphate transport systems in wild-type cells grown at different pH values was quantified. The contribution of the Na(+)-coupled transport system to the total cellular phosphate uptake activity increases progressively with increasing pH. |
| Author | Lundh, Fredrik Thevelein, Johan M. Pattison-Granberg, Johanna Mouillon, Jean-Marie Samyn, Dieter Persson, Bengt L. Popova, Yulia Zvyagilskaya, Renata A. |
| Author_xml | – sequence: 1 givenname: Renata A. surname: Zvyagilskaya fullname: Zvyagilskaya, Renata A. organization: A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect, Moscow, Russia – sequence: 2 givenname: Fredrik surname: Lundh fullname: Lundh, Fredrik organization: School of Pure and Applied Natural Sciences, Kalmar University, Kalmar, Sweden – sequence: 3 givenname: Dieter surname: Samyn fullname: Samyn, Dieter organization: School of Pure and Applied Natural Sciences, Kalmar University, Kalmar, Sweden – sequence: 4 givenname: Johanna surname: Pattison-Granberg fullname: Pattison-Granberg, Johanna organization: School of Pure and Applied Natural Sciences, Kalmar University, Kalmar, Sweden – sequence: 5 givenname: Jean-Marie surname: Mouillon fullname: Mouillon, Jean-Marie organization: School of Pure and Applied Natural Sciences, Kalmar University, Kalmar, Sweden – sequence: 6 givenname: Yulia surname: Popova fullname: Popova, Yulia organization: Laboratory of Molecular Cell Biology, Institute of Botany and Microbiology, Katholieke Universiteit Leuven, Arenberg, Leuven-Heverlee, Flanders, Belgium – sequence: 7 givenname: Johan M. surname: Thevelein fullname: Thevelein, Johan M. organization: Laboratory of Molecular Cell Biology, Institute of Botany and Microbiology, Katholieke Universiteit Leuven, Arenberg, Leuven-Heverlee, Flanders, Belgium – sequence: 8 givenname: Bengt L. surname: Persson fullname: Persson, Bengt L. email: bengt.persson@hik.se organization: School of Pure and Applied Natural Sciences, Kalmar University, Kalmar, Sweden |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18625026$$D View this record in MEDLINE/PubMed https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-1813$$DView record from Swedish Publication Index (Linnéuniversitetet) https://urn.kb.se/resolve?urn=urn:nbn:se:oru:diva-112533$$DView record from Swedish Publication Index (Örebro universitet) |
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| Copyright | 2008 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2008 2008 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved |
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| Notes | Editor: André Goffeau Johanna Pattison‐Granberg, Sweden Recycling AB, Järnvägsgatan 19, S‐360 51 Hovmantorp, Sweden. Jean‐Marie Mouillon, Fluxome Sciences A/S, Diplomvej 378, D‐2800 Kgs. Lyngby, Denmark. Present addresses ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
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| Snippet | Abstract
The Na+-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of... The Na+‐coupled, high‐affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low... The Na(+)-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low... The Na+-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low... The Na⁺-coupled, high-affinity Pho89 plasma membrane phosphate transporter in Saccharomyces cerevisiae has so far been difficult to study because of its low... |
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| SubjectTerms | Affinity Biochemistry Biokemi Carbonyl compounds Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology Clonal deletion Cyanides Gene Deletion Gene Dosage genes Hydrogen-Ion Concentration ions Kinetics pH effects PHO pathway Pho89 Phosphate Phosphate Transport Proteins - genetics Phosphate transporter Phosphate uptake system Phosphates Phosphates - metabolism plasma membrane Protein folding protons Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism sodium Sodium - metabolism Sodium-Phosphate Cotransporter Proteins, Type III - genetics Sodium-Phosphate Cotransporter Proteins, Type III - metabolism Uncoupling Agents - pharmacology Yeast yeasts |
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| Title | Characterization of the Pho89 phosphate transporter by functional hyperexpression in Saccharomyces cerevisiae |
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