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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

PHO4  -  Pho4p

Saccharomyces cerevisiae S288c

Synonyms: Phosphate system positive regulatory protein PHO4, YFR034C
 
 
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Disease relevance of PHO4

  • Upon derepression of PHO8, the chromatin structure changes significantly: The two upstream hypersensitive sites containing the PHO4 binding sites merge, resulting in a long region of hypersensitivity [1].
  • Chromatin reorganization of the PHO5 and murine mammary tumor virus (MMTV) promoters is triggered by binding of either Pho4 or the glucocorticoid receptor (GR), respectively [2].
 

High impact information on PHO4

 

Biological context of PHO4

 

Anatomical context of PHO4

  • We conclude that the vac5-1 allele directs the Pho85 kinase to regulate, via transcription factors Pho4 and Pho2, genes that affect vacuole inheritance but which are not known to be under normal PHO pathway control [10].
 

Associations of PHO4 with chemical compounds

  • In addition, we also demonstrate that an additional factor, Pho81, interacts in high phosphate with both the Pho80 cyclin and with Pho4 [11].
  • PHO4 binding specificity is altered by mutation at any of three different positions in the basic region, including a single Glu to Asp substitution [12].
  • PHO4 binds to DNA as a homodimer with direct reading of both the core E-box sequence CACGTG and its 3'-flanking bases [13].
  • We have identified a genetic locus, pho4, in Schizosaccharomyces pombe which encodes a minor expressed cell surface acid phosphatase that is repressed by low concentrations (0.5 microM) of thiamin [14].
  • A cysteine residue in helixII of the bHLH domain is essential for homodimerization of the yeast transcription factor Pho4p [15].
 

Physical interactions of PHO4

 

Enzymatic interactions of PHO4

  • Furthermore, immunoprecipitated Pcl9 complexes from yeast lysates were capable of phosphorylating the exogenous substrate Pho4 [20].
 

Regulatory relationships of PHO4

  • More detailed investigation of APase synthesis is a conditional PHO80(Ts) mutant indicated that neither PHO4 nor any other protein factor necessary for APase mRNA synthesis is transcriptionally regulated by PHO80 [21].
  • Phosphorylation of Pho4 inhibits its interaction with Pse1, providing a mechanism by which phosphorylation may regulate import of Pho4 in vivo [5].
  • In every case, the ability of the Pho4 mutants to activate transcription correlates with their ability to disrupt nucleosome structure in the PHO5 promoter [22].
  • Expression of VTC4 is regulated by Pho4, a transcription factor that is inhibited by the Pho80-Pho85 kinase [23].
  • The ability of Pho85 to regulate the transcription factor Pho4 is mediated by its association the Pho80 cyclin [24].
 

Other interactions of PHO4

  • Analysis of the sequence data uncovered striking homology regions with PHO4, another protein necessary for the induction of PHO5 [25].
  • Deletion of PHO4 abolished GIT1 transcription in a wild-type strain [26].
  • PHO86 has two putative binding sites for the transcriptional activator, Pho4p, at nucleotide positions -191 and -497 relative to the ATG start codon, and showed substantial levels of transcription under high-P(i) conditions and more enhanced levels in low-P(i) medium [27].
  • In low phosphate, Pho80 and Pho81 dissociate from Pho4, but retain the ability to interact with each other [11].
  • NIN1 is mapped on chromosome VI, 16 cM centromere-distal to PHO4 [28].
 

Analytical, diagnostic and therapeutic context of PHO4

References

  1. Activation of the weakly regulated PHO8 promoter in S. cerevisiae: chromatin transition and binding sites for the positive regulatory protein PHO4. Barbarić, S., Fascher, K.D., Hörz, W. Nucleic Acids Res. (1992) [Pubmed]
  2. Comparison of nucleosome remodeling by the yeast transcription factor Pho4 and the glucocorticoid receptor. Then Bergh, F., Flinn, E.M., Svaren, J., Wright, A.P., Hörz, W. J. Biol. Chem. (2000) [Pubmed]
  3. Roles of phosphorylation sites in regulating activity of the transcription factor Pho4. Komeili, A., O'Shea, E.K. Science (1999) [Pubmed]
  4. Phosphate-regulated inactivation of the kinase PHO80-PHO85 by the CDK inhibitor PHO81. Schneider, K.R., Smith, R.L., O'Shea, E.K. Science (1994) [Pubmed]
  5. Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Kaffman, A., Rank, N.M., O'Shea, E.K. Genes Dev. (1998) [Pubmed]
  6. Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae. Ogawa, N., Oshima, Y. Mol. Cell. Biol. (1990) [Pubmed]
  7. Possible cross-regulation of phosphate and sulfate metabolism in Saccharomyces cerevisiae. O'Connell, K.F., Baker, R.E. Genetics (1992) [Pubmed]
  8. Interaction of Saccharomyces cerevisiae Pho2 with Pho4 increases the accessibility of the activation domain of Pho4. Shao, D., Creasy, C.L., Bergman, L.W. Mol. Gen. Genet. (1996) [Pubmed]
  9. A small protein (Ags1p) and the Pho80p-Pho85p kinase complex contribute to aminoglycoside antibiotic resistance of the yeast Saccharomyces cerevisiae. Wickert, S., Finck, M., Herz, B., Ernst, J.F. J. Bacteriol. (1998) [Pubmed]
  10. A truncated form of the Pho80 cyclin redirects the Pho85 kinase to disrupt vacuole inheritance in S. cerevisiae. Nicolson, T.A., Weisman, L.S., Payne, G.S., Wickner, W.T. J. Cell Biol. (1995) [Pubmed]
  11. The transcription factor, the Cdk, its cyclin and their regulator: directing the transcriptional response to a nutritional signal. Hirst, K., Fisher, F., McAndrew, P.C., Goding, C.R. EMBO J. (1994) [Pubmed]
  12. Single amino acid substitutions alter helix-loop-helix protein specificity for bases flanking the core CANNTG motif. Fisher, F., Goding, C.R. EMBO J. (1992) [Pubmed]
  13. Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition. Shimizu, T., Toumoto, A., Ihara, K., Shimizu, M., Kyogoku, Y., Ogawa, N., Oshima, Y., Hakoshima, T. EMBO J. (1997) [Pubmed]
  14. Identification and characterization of thiamin repressible acid phosphatase in yeast. Schweingruber, M.E., Fluri, R., Maundrell, K., Schweingruber, A.M., Dumermuth, E. J. Biol. Chem. (1986) [Pubmed]
  15. A cysteine residue in helixII of the bHLH domain is essential for homodimerization of the yeast transcription factor Pho4p. Shao, D., Creasy, C.L., Bergman, L.W. Nucleic Acids Res. (1998) [Pubmed]
  16. The two positively acting regulatory proteins PHO2 and PHO4 physically interact with PHO5 upstream activation regions. Vogel, K., Hörz, W., Hinnen, A. Mol. Cell. Biol. (1989) [Pubmed]
  17. Specific cis-acting sequence for PHO8 expression interacts with PHO4 protein, a positive regulatory factor, in Saccharomyces cerevisiae. Hayashi, N., Oshima, Y. Mol. Cell. Biol. (1991) [Pubmed]
  18. Glycerophosphoinositol, a novel phosphate source whose transport is regulated by multiple factors in Saccharomyces cerevisiae. Almaguer, C., Cheng, W., Nolder, C., Patton-Vogt, J. J. Biol. Chem. (2004) [Pubmed]
  19. Increasing the rate of chromatin remodeling and gene activation--a novel role for the histone acetyltransferase Gcn5. Barbaric, S., Walker, J., Schmid, A., Svejstrup, J.Q., Hörz, W. EMBO J. (2001) [Pubmed]
  20. A role for the Pcl9-Pho85 cyclin-cdk complex at the M/G1 boundary in Saccharomyces cerevisiae. Tennyson, C.N., Lee, J., Andrews, B.J. Mol. Microbiol. (1998) [Pubmed]
  21. Regulation of repressible acid phosphatase gene transcription in Saccharomyces cerevisiae. Lemire, J.M., Willcocks, T., Halvorson, H.O., Bostian, K.A. Mol. Cell. Biol. (1985) [Pubmed]
  22. The transactivation domain of Pho4 is required for nucleosome disruption at the PHO5 promoter. Svaren, J., Schmitz, J., Hörz, W. EMBO J. (1994) [Pubmed]
  23. Dissection of a complex phenotype by functional genomics reveals roles for the yeast cyclin-dependent protein kinase Pho85 in stress adaptation and cell integrity. Huang, D., Moffat, J., Andrews, B. Mol. Cell. Biol. (2002) [Pubmed]
  24. Regulation of the Pcl7-Pho85 cyclin-cdk complex by Pho81. Lee, M., O'Regan, S., Moreau, J.L., Johnson, A.L., Johnston, L.H., Goding, C.R. Mol. Microbiol. (2000) [Pubmed]
  25. The sequence of the Saccharomyces cerevisiae gene PHO2 codes for a regulatory protein with unusual aminoacid composition. Sengstag, C., Hinnen, A. Nucleic Acids Res. (1987) [Pubmed]
  26. Inositol and phosphate regulate GIT1 transcription and glycerophosphoinositol incorporation in Saccharomyces cerevisiae. Almaguer, C., Mantella, D., Perez, E., Patton-Vogt, J. Eukaryotic Cell (2003) [Pubmed]
  27. A putative new membrane protein, Pho86p, in the inorganic phosphate uptake system of Saccharomyces cerevisiae. Yompakdee, C., Bun-ya, M., Shikata, K., Ogawa, N., Harashima, S., Oshima, Y. Gene (1996) [Pubmed]
  28. A new essential gene of Saccharomyces cerevisiae, a defect in it may result in instability of nucleus. Nisogi, H., Kominami, K., Tanaka, K., Toh-e, A. Exp. Cell Res. (1992) [Pubmed]
  29. The transcriptional activators of the PHO regulon, Pho4p and Pho2p, interact directly with each other and with components of the basal transcription machinery in Saccharomyces cerevisiae. Magbanua, J.P., Ogawa, N., Harashima, S., Oshima, Y. J. Biochem. (1997) [Pubmed]
  30. Functional domains of the transcriptional activator NUC-1 in Neurospora crassa. Kang, S. Gene (1993) [Pubmed]
 
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