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  • 1
    Electronic Resource
    Electronic Resource
    Two new genes, PHO86 and PHO87, involved in inorganic phosphate uptake in Saccharomyces cerevisiae (1996)
    Springer
    Current genetics 29 (1996), S. 344-351 
    Details
    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
    URL: http://dx.doi.org/10.1007/s002940050055
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  • 2
    Electronic Resource
    Electronic Resource
    The role of cysteine residues in the homeodomain protein Matα2 in mating-type control of Saccharomyces cerevisiae (1997)
    Springer
    Molecular genetics and genomics 255 (1997), S. 166-171 
    Details
    ISSN: 1617-4623
    Keywords: Key words Homeodomain protein ; Mating-type control ; Matα2 ; Disulfide bond ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Matα2 homeodomain protein plays a pivotal role in the control of cell type in Saccharomyces cerevisiae. The homeodomain in the C-terminal region of Matα2 functions as a DNA-binding domain and the N-terminal region, containing two cysteine residues at positions 33 and 34, is thought to be involved in formation of Matα2 homodimers via disulfide bonds. matα2 mutants, isolated in a previous study, in which haploid-specific genes cannot be repressed by the Mata1-Matα2 heterodimer but a-specific genes can be repressed by the Matα2 homodimer, were found to produce mutant Matα2 with a substitution of tyrosine or phenylalanine for Cys33. To clarify the role of Cys33 and Cys34 in the Matα2 protein, we generated several matα2 mutants by site-directed mutagenesis which had serine residues in place of these Cys residues. Transforming MAT a cells with plasmids carrying these matα2 (MATα1 +) mutations rendered transformants unable to mate. Northern blot analysis revealed that transcription of the a-specific gene STE2 and the haploid-specific locus RME1 in these transformants is repressed to the same level as in wild-type MAT a/MATα cells. We concluded that neither Cys33 nor Cys34 is required for repression of a-specific genes by the Matα2 homodimer or of haploid-specific genes by the Mata1-Matα2 heterodimer, and therefore suggest that Matα2 homodimer formation in vivo is not mediated by disulfide linkage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050485
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  • 3
    Electronic Resource
    Electronic Resource
    A putative membrane protein, Pho88p, involved in inorganic phosphate transport inSaccharomyces cerevisiae (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 580-590 
    Details
    ISSN: 1617-4623
    Keywords: 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 ofSaccharomyces cerevisiae is repressed by inorganic phosphate (Pi) in the medium via that same regulatory system. The activity of Pho81p, the product ofPHO81, is also inhibited by a high concentration of Pi in the medium. Increased dosage ofPHO86, a gene encoding a putative membrane protein associated with a Pi transporter complex, activates the Pi-inhibited Pho81p produced under the control of theGAL1 promoter. A new gene,PHO88/YBR106w, has now been identified as a multicopy suppressor of the rAPase− phenotype of the cells caused by theP i inhibition of Pho81p. Thepho86 disruptant expressed rAPase activity in high-Pi medium, while thepho88 disruptant did not. The Δpho86 Δpho88 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 ofPHO88 orPHO86 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
    URL: http://dx.doi.org/10.1007/BF02173648
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  • 4
    Electronic Resource
    Electronic Resource
    A putative membrane protein, Pho88p, involved in inorganic phosphate transport in Saccharomyces cerevisiae (1996)
    Springer
    Molecular genetics and genomics 251 (1996), S. 580-590 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02173648
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