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

Jens O Lagerstedt, Ian Reeve, John C Voss, Bengt L Persson

Research output: Contribution to journalArticlepeer-review

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 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.

Original languageEnglish
Pages (from-to)511-7
JournalBiochemistry
Volume44
Issue number2
DOIs
Publication statusPublished - 2005 Jan 18
Externally publishedYes

Free 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

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