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The structure and function of GTP binding protein Gtr1 and its role in phosphate transport in Saccharomyces cerevisiae
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2005 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 2, 511-517 p.Article in journal (Refereed) Published
Abstract [en]

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 Δgtr1 similar to the Δpho84 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.

Place, publisher, year, edition, pages
2005. Vol. 44, no 2, 511-517 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:su:diva-23329DOI: 10.1021/bi048659vOAI: oai:DiVA.org:su-23329DiVA: diva2:191380
Note
Part of urn:nbn:se:su:diva-240Available from: 2004-09-16 Created: 2004-09-16 Last updated: 2017-12-13Bibliographically approved
In thesis
1. Regulatory and Structural Properties of the High-Affinity Phosphate Acquisition System in Saccharomyces cerevisiae
Open this publication in new window or tab >>Regulatory and Structural Properties of the High-Affinity Phosphate Acquisition System in Saccharomyces cerevisiae
2004 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Inorganic phosphate is an essential nutrient required for the synthesis of many cellular components (e.g., nucleic acids, proteins, lipids and sugars), as well as for meeting metabolic needs (e.g., energy production and translocation). In the case of the unicellular yeast Saccharomyces cerevisiae, the presence of both high- and low-affinity phosphate transporters in the plasma membrane provides for adaptation to environmental variations. Of these systems, the high-affinity Pho84 transport system is the major phosphate transporter activated when the cells have limited access to external phosphate.

This integral membrane protein belongs to the major facilitator superfamily (MFS) and possesses 12 predicted transmembrane domains. Activation of this and other proteins (e.g., extracellular phosphatases) involved in maintaining cellular phosphate homeostasis under conditions of limited availability of external phosphate is controlled primarily by transcriptional regulation. However, the presence of proteins indirectly or directly involved in phosphate transport by Pho84, including Gtr1, has been reported. The Gtr1 protein binds guanine nucleotides and probably functions as a molecular switch.

The present thesis describes the regulated intracellular trafficking and degradation of Pho84 in response to phosphate, as well as to its non-hydrolysable and non-utilizable analog methylphosphonate. The involvement of the Gtr1 protein in high-affinity phosphate uptake has also been examined. Moreover, in vitro and in silico analyses of structural and functional aspects of both the Pho84 and Gtr1 proteins are presented and discussed.

Place, publisher, year, edition, pages
Stockholm: Institutionen för biokemi och biofysik, 2004. 63 p.
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:su:diva-240 (URN)91-7265-936-X (ISBN)
Public defence
2004-10-07, William-Olssonsalen, Geovetenskapens hus, Svante Arrhenius väg 8 A, Stockholm, 10:00
Opponent
Supervisors
Available from: 2004-09-16 Created: 2004-09-16Bibliographically approved

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Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

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