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  • 1
    ISSN: 1432-0983
    Keywords: Key words Arsenate resistance ; Phosphatase regulation ; Pi-transporter ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The PHO84 gene in Saccharomyces cerevisiae encodes a Pi transporter, mutation of which confers constitutive synthesis of repressible acid phosphatase (rAPase), in medium containing repressible amounts of Pi, and an arsenate-resistant phenotype. We selected an arsenate-resistant mutant showing the constitutive synthesis of rAPase on nutrient plates containing 4.5 mM arsenate. This mutant has double mutations designated as pho86 and pho87. The mutant transcribes PHO84 even in the repressible condition but has a severe defect in Pi uptake. The constitutive rAPase+ phenotype of the pho86 pho87 mutant was partially suppressed by an increased dosage of the PHO84 gene. The PHO87 gene was found to be identical with YCR524, according to the published nucleotide sequence of chromosome III, which encodes a protein of 923 amino-acid residues with a highly charged N-terminal half followed by a C-terminal half consisting of 12 membrane-spanning segments as in Pho84p. These and the other findings suggest that the Pho86p and Pho87p proteins collaborate with Pho84p in Pi uptake.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0983
    Keywords: Arsenate resistance ; Phosphatase regulation ; Pi-transporter ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract ThePHO84 gene inSaccharomyces cerevisiae encodes a Pi transporter, mutation of which confers constitutive synthesis of repressible acid phosphatase (rAPase), in medium containing repressible amounts of Pi, and an arsenate-resistant phenotype. We selected an arsenate-resistant mutant showing the constitutive synthesis of rAPase on nutrient plates containing 4.5 mM arsenate. This mutant has double mutations designated aspho86 andpho87. The mutant transcribesPHO84 even in the repressible condition but has a severe defect in Pi uptake. The constitutive rAPase+ phenotype of thepho86 pho87 mutant was partially suppressed by an increased dosage of thePHO84 gene. ThePHO87 gene was found to be identical withYCR524, according to the published nucleotide sequence of chromosome III, which encodes a protein of 923 amino-acid residues with a highly charged N-terminal half followed by a C-terminal half consisting of 12 membrane-spanning segments as in Pho84p. These and the other findings suggest that the Pho86p and Pho87p proteins collaborate with Pho84p in Pi uptake.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    ISSN: 1617-4623
    Keywords: Key words Membrane proteins ; Phosphatase regulation ; Pho88p ; Pi transporter ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Transcription of a regulatory gene, PHO81, in the phosphatase regulon of Saccharomyces cerevisiae is repressed by inorganic phosphate (Pi) in the medium via that same regulatory system. The activity of Pho81p, the product of PHO81, is also inhibited by a high concentration of Pi in the medium. Increased dosage of PHO86, a gene encoding a putative membrane protein associated with a Pi transporter complex, activates the Pi-inhibited Pho81p produced under the control of the GAL1 promoter. A new gene, PHO88/ YBR106w, has now been identified as a multicopy suppressor of the rAPase- phenotype of the cells caused by the P i inhibition of Pho81p. The pho86 disruptant expressed rAPase activity in high-Pi medium, while the pho88 disruptant did not. The Δpho86Δpho88 double disruption resulted in enhanced synthesis of rAPase under the high-Pi condition and conferred arsenate resistance on the cells than those in single disruptants of these genes. Its hydropathy profile and the results of an analysis of its cellular localization suggested that Pho88p is a membrane protein similar to Pho86p. Both disruption and high dosage of PHO88 or PHO86 resulted in reduced Pi uptake. These findings suggest that Pho88p is also involved in Pi transport and modulates Pho81p function together with Pho86p.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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