Structure and function of the GTP binding protein Gtr1 and its role in phosphate transport in Saccharomyces cerevisiae
(2005) In Biochemistry 44(2). p.7-511- Abstract
The Pho84 high-affinity phosphate permease is the primary phosphate transporter in the yeast Saccharomyces cerevisiae under phosphate-limiting conditions. The soluble G protein, Gtr1, has previously been suggested to be involved in the derepressible Pho84 phosphate uptake function. This idea was based on a displayed deletion phenotype of Deltagtr1 similar to the Deltapho84 phenotype. As of yet, the mode of interaction has not been described. The consequences of a deletion of gtr1 on in vivo Pho84 expression, trafficking and activity, and extracellular phosphatase activity were analyzed in strains synthesizing either Pho84-green fluorescent protein or Pho84-myc chimeras. The studies revealed a delayed response in Pho84-mediated phosphate... (More)
The Pho84 high-affinity phosphate permease is the primary phosphate transporter in the yeast Saccharomyces cerevisiae under phosphate-limiting conditions. The soluble G protein, Gtr1, has previously been suggested to be involved in the derepressible Pho84 phosphate uptake function. This idea was based on a displayed deletion phenotype of Deltagtr1 similar to the Deltapho84 phenotype. As of yet, the mode of interaction has not been described. The consequences of a deletion of gtr1 on in vivo Pho84 expression, trafficking and activity, and extracellular phosphatase activity were analyzed in strains synthesizing either Pho84-green fluorescent protein or Pho84-myc chimeras. The studies revealed a delayed response in Pho84-mediated phosphate uptake and extracellular phosphatase activity under phosphate-limiting conditions. EPR spectroscopic studies verified that the N-terminal G binding domain (residues 1-185) harbors the nucleotide responsive elements. In contrast, the spectra obtained for the C-terminal part (residues 186-310) displayed no evidence of conformational changes upon GTP addition.
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- author
- Lagerstedt, Jens O LU ; Reeve, Ian ; Voss, John C LU and Persson, Bengt L
- publishing date
- 2005-01-18
- type
- Contribution to journal
- publication status
- published
- keywords
- Electron Spin Resonance Spectroscopy, Gene Deletion, Green Fluorescent Proteins, Models, Molecular, Monomeric GTP-Binding Proteins, Phosphates, Protein Binding, Protein Conformation, Protein Transport, Proton-Phosphate Symporters, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Thermodynamics, Journal Article, Research Support, Non-U.S. Gov't
- in
- Biochemistry
- volume
- 44
- issue
- 2
- pages
- 7 - 511
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:15641775
- scopus:12144252921
- ISSN
- 0006-2960
- DOI
- 10.1021/bi048659v
- language
- English
- LU publication?
- no
- id
- 88be7182-78e0-4aca-ab6c-1cca762c67a0
- date added to LUP
- 2017-10-19 20:10:54
- date last changed
- 2024-10-14 15:37:58
@article{88be7182-78e0-4aca-ab6c-1cca762c67a0, abstract = {{<p>The Pho84 high-affinity phosphate permease is the primary phosphate transporter in the yeast Saccharomyces cerevisiae under phosphate-limiting conditions. The soluble G protein, Gtr1, has previously been suggested to be involved in the derepressible Pho84 phosphate uptake function. This idea was based on a displayed deletion phenotype of Deltagtr1 similar to the Deltapho84 phenotype. As of yet, the mode of interaction has not been described. The consequences of a deletion of gtr1 on in vivo Pho84 expression, trafficking and activity, and extracellular phosphatase activity were analyzed in strains synthesizing either Pho84-green fluorescent protein or Pho84-myc chimeras. The studies revealed a delayed response in Pho84-mediated phosphate uptake and extracellular phosphatase activity under phosphate-limiting conditions. EPR spectroscopic studies verified that the N-terminal G binding domain (residues 1-185) harbors the nucleotide responsive elements. In contrast, the spectra obtained for the C-terminal part (residues 186-310) displayed no evidence of conformational changes upon GTP addition.</p>}}, author = {{Lagerstedt, Jens O and Reeve, Ian and Voss, John C and Persson, Bengt L}}, issn = {{0006-2960}}, keywords = {{Electron Spin Resonance Spectroscopy; Gene Deletion; Green Fluorescent Proteins; Models, Molecular; Monomeric GTP-Binding Proteins; Phosphates; Protein Binding; Protein Conformation; Protein Transport; Proton-Phosphate Symporters; Recombinant Fusion Proteins; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship; Thermodynamics; Journal Article; Research Support, Non-U.S. Gov't}}, language = {{eng}}, month = {{01}}, number = {{2}}, pages = {{7--511}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Biochemistry}}, title = {{Structure and function of the GTP binding protein Gtr1 and its role in phosphate transport in Saccharomyces cerevisiae}}, url = {{http://dx.doi.org/10.1021/bi048659v}}, doi = {{10.1021/bi048659v}}, volume = {{44}}, year = {{2005}}, }