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Structure and function of the GTP binding protein Gtr1 and its role in phosphate transport in Saccharomyces cerevisiae

Lagerstedt, Jens O LU ; Reeve, Ian; Voss, John C LU and Persson, Bengt L (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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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
external identifiers
  • 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
2017-10-23 09:53:39
@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},
  keyword      = {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},
  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},
  volume       = {44},
  year         = {2005},
}