The structure and function of GTP binding protein Gtr1 and its role in phosphate transport in Saccharomyces cerevisiae
2005 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 2, 511-517 p.Article in journal (Refereed) Published
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.
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
IdentifiersURN: urn:nbn:se:su:diva-23329DOI: 10.1021/bi048659vOAI: oai:DiVA.org:su-23329DiVA: diva2:191380
Part of urn:nbn:se:su:diva-2402004-09-162004-09-162010-08-09Bibliographically approved