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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 21 (1992), S. 95-99 
    ISSN: 1432-0983
    Keywords: PHO ; Saccharomyces ; Protein-protein interaction ; Regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have isolated suppressors of a PHO4 c (a positive regulator) mutant which normally confers weak constitutivity for acid phosphatase production on the Saccharomyces cell. One dominant suppressor (PHO80-2) was found to be an allele of PHO80 (a negative regulator) that changes G to A, resulting in substitution of isoleucine for methionine 42 of the Pho80 protein. Substitution of valine (PHO80-3) or leucine (PHO80-4) for the same methionine by site-directed mutagenesis also suppressed PHO c. Suppression by PHO80-2) did show some allele specificity. From these results we were able to delimit the region of PHo80 which may interact with the Pho4 protein.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 231 (1992), S. 426-432 
    ISSN: 1617-4623
    Keywords: PHO ; PHO85 ; Protein kinase ; S. cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Both PHO80 and PHO85 genes are required to establish the repressed state of the PHO system of Saccharomyces cerevisiae. S1 nuclease protection analysis of the PHO85 transcript revealed that the PHO85 gene contains an intron at the 6th codon of the gene. Each of the fusion proteins, LacZ-Pho80 and LacZ-Pho85, was produced into Escherichia coli and used as an antigen to raise antibodies in a rabbit. Using the affinity-purified antibodies in Western blotting experiments, the PHO85 protein was detected as a 36 kDa and the PHO80 protein as a 34 kDa protein. The PHO80 protein was detected only in extracts prepared from an overproducing strain. The immunoprecipitate containing the PHO85 protein showed protein kinase activity suggesting that PHO85 is a protein kinase gene, which is consistent with the observation that the deduced amino acid sequence of the PHO85 protein resembles that of some protein kinases. The PHO80 protein was found to be phosphorylated in the presence of PHO85 protein.
    Type of Medium: Electronic Resource
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