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PHO5  -  Pho5p

Saccharomyces cerevisiae S288c

Synonyms: P60, Repressible acid phosphatase, YBR0814, YBR093C
 
 
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Disease relevance of PHO5

 

High impact information on PHO5

  • We examine transcriptional activation and chromatin remodeling at the PHO5 promoter in yeast by fusion proteins that are thought to act by recruiting the RNA polymerase II holoenzyme to DNA in the absence of a classic activating region [5].
  • To investigate the mechanism, we replaced the PHO80 gene, a negative regulator of PHO5, by a temperature-sensitive allele [6].
  • Nucleosome disruption at the yeast PHO5 promoter upon PHO5 induction occurs in the absence of DNA replication [6].
  • This activation is specific since other regulated genes (GAL10, PHO5, CUP1) are repressed and induced normally in these cells [7].
  • We have determined whether acetylation and deacetylation are promoter specific at PHO5, by using antibodies against acetylated lysine residues and chromatin immunoprecipitation to examine the acetylation state of a 4.25-kilobase region surrounding the PHO5 gene [8].
 

Chemical compound and disease context of PHO5

  • For this purpose a cassette was constructed which contains the E. coli hph gene, conferring hygromycin B resistance, fused to the 5' expression signals of the A. adeninivorans TEF1 gene, encoding the translation elongation factor EF-1alpha, and the transcription termination region of the Saccharomyces cerevisiae PHO5 gene [9].
 

Biological context of PHO5

  • Here, we show that the PHO5 promoter nucleosomes are reassembled concomitant with transcriptional repression and displacement of the TATA binding protein and RNA polymerase II (RNA Pol II) [10].
  • This delay in transcriptional activation is specifically due to slow chromatin remodeling of the PHO5 promoter, whereas the transmission of the phosphate starvation signal to the PHO5 promoter progresses at a normal rate [11].
  • Subcloning of partial Sau3A digests and functional in vivo analysis by transformation together with DNA sequence analysis showed that the two genes are oriented in the order (5') PHO5 , PHO3 (3') [12].
  • To test this hypothesis, we used our recently established yeast extract in vitro chromatin assembly system, which generates the characteristic PHO5 promoter chromatin [13].
  • Polyphosphate levels also fluctuate inversely with PHO5 mRNA during the cell cycle, further substantiating an antagonistic link between this phosphate polymer and PHO5 mitotic regulation [14].
 

Anatomical context of PHO5

  • The repressible Saccharomyces cerevisiae acid phosphatase (APase) coded by the PHO5 gene is a cell wall glycoprotein that follows the yeast secretory pathway [15].
  • As a first step, we have asked whether the characteristic PHO5 promoter chromatin structure depends on the cellular context including replication or higher order nuclear chromatin organization or whether it can be reconstituted in vitro in a cell-free system [16].
  • The gene PHO5 coding for one of the repressible acid phosphatases of the yeast Saccharomyces cerevisiae has been expressed at high efficiency in the baby hamster kidney (BHK) cell line [17].
 

Associations of PHO5 with chemical compounds

  • Orthophosphate addition, however, represses mitotic PHO5 expression in a phm3delta strain [14].
  • Overexpression of unrelated phosphate transporters or a glycerophosphoinositol transporter in the pho84Delta strain suppresses the PHO5 constitutive phenotype [18].
  • It was found that glucose arrest led to a severe disruption in PHO5 chromatin structure and that most nucleosomes had their position altered or were lost from the PHO5 promoter region [19].
  • In addition, four other classes of mutants, nfo1, nfo2, nfo3 and nfo4 (negative factor for OLE1) mutants that have mutations causing strong expression of the OLE1p-PHO5 fusion gene under repression conditions (presence of oleic acid), were isolated [20].
  • Specific purine-pyrimidine motifs (RRYRR) (R = purine and Y = pyrimidine) serve as PHO5 mRNA initiation sites, but only if they lie 55-110 bp downstream of a functional TATA element [21].
 

Physical interactions of PHO5

  • The two positively acting regulatory proteins PHO2 and PHO4 physically interact with PHO5 upstream activation regions [22].
 

Regulatory relationships of PHO5

  • Cells carrying a disruption of the PHO85 gene inappropriately express both PHO5 and GSY2, resulting in the increase in phosphate scavenging and hyperaccumulation of glycogen in nutrient-rich conditions [23].
  • Transcriptional regulation of the yeast PHO8 promoter in comparison to the coregulated PHO5 promoter [24].
  • The rho- mutation also increased the expression of the PHO5 gene under the control of the HIS5 promoter in a plasmid and the ACT1 gene in the yeast chromosome, but did not increase the expression of the ribosomal RNA gene [25].
  • We have investigated the role of the HAT Gcn5 at the nucleosomally regulated PHO5 promoter [26].
  • In every case, the ability of the Pho4 mutants to activate transcription correlates with their ability to disrupt nucleosome structure in the PHO5 promoter [27].
 

Other interactions of PHO5

  • Here we show that even though the steady-state level of activated PHO5 transcription is not affected by deletion of GCN5, the rate of activation following phosphate starvation is significantly decreased [11].
  • In addition, rpd3 deletions retard full induction of the PHO5 promoter fused to the reporter lacZ [28].
  • An SPT3 deletion severely compromises the PHO5 promoter and reduces the extent of transcriptional activation by diminishing the binding of the TATA binding protein to the promoter without, however, affecting the rate or the extent of chromatin remodeling [29].
  • Analysis of the sequence data uncovered striking homology regions with PHO4, another protein necessary for the induction of PHO5 [30].
  • The cyclin-dependent protein kinase Pho85 is a known negative regulatory factor for two stress response genes, PHO5 and GSY2, which encode the inducible form of acid phosphatase and glycogen synthase, respectively, in the yeast Saccharomyces cerevisiae [23].
  • The snf2 ino80 double mutation had a synthetic kinetic effect but eventually still allowed strong PHO5 induction [31].
 

Analytical, diagnostic and therapeutic context of PHO5

  • A gel retardation assay with beta-galactosidase::PHO4 fused protein revealed that the 85-aa C terminus is the domain responsible for binding to the promoter DNA of PHO5, a gene under the control of PHO4 [32].
  • The values of Mr estimated by HPLC chromatography for the enzymes encoded for by the genes PHO5, PHO10 and PHO11 and SDS-polyacrilamide gel electrophoresis data suggested an oligomeric organisation of the enzymes [33].

References

  1. 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]
  2. Cloning, sequencing, and characterization of the principal acid phosphatase, the phoC+ product, from Zymomonas mobilis. Pond, J.L., Eddy, C.K., Mackenzie, K.F., Conway, T., Borecky, D.J., Ingram, L.O. J. Bacteriol. (1989) [Pubmed]
  3. Raf60, a novel component of the Rpd3 histone deacetylase complex required for Rpd3 activity in Saccharomyces cerevisiae. Colina, A.R., Young, D. J. Biol. Chem. (2005) [Pubmed]
  4. Characteristics of hepatitis B surface antigen produced in yeast. Choo, K.B., Wu, S.M., Lee, H.H., Lo, S.C. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  5. RNA polymerase II holoenzyme recruitment is sufficient to remodel chromatin at the yeast PHO5 promoter. Gaudreau, L., Schmid, A., Blaschke, D., Ptashne, M., Hörz, W. Cell (1997) [Pubmed]
  6. Nucleosome disruption at the yeast PHO5 promoter upon PHO5 induction occurs in the absence of DNA replication. Schmid, A., Fascher, K.D., Hörz, W. Cell (1992) [Pubmed]
  7. Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast. Kayne, P.S., Kim, U.J., Han, M., Mullen, J.R., Yoshizaki, F., Grunstein, M. Cell (1988) [Pubmed]
  8. Global histone acetylation and deacetylation in yeast. Vogelauer, M., Wu, J., Suka, N., Grunstein, M. Nature (2000) [Pubmed]
  9. Integrative transformation of the dimorphic yeast arxula adeninivorans LS3 based on hygromycin B resistance. Rösel, H., Kunze, G. Curr. Genet. (1998) [Pubmed]
  10. Transcriptional activators are dispensable for transcription in the absence of Spt6-mediated chromatin reassembly of promoter regions. Adkins, M.W., Tyler, J.K. Mol. Cell (2006) [Pubmed]
  11. 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]
  12. Two yeast acid phosphatase structural genes are the result of a tandem duplication and show different degrees of homology in their promoter and coding sequences. Meyhack, B., Bajwa, W., Rudolph, H., Hinnen, A. EMBO J. (1982) [Pubmed]
  13. Nucleosome stability at the yeast PHO5 and PHO8 promoters correlates with differential cofactor requirements for chromatin opening. Hertel, C.B., Längst, G., Hörz, W., Korber, P. Mol. Cell. Biol. (2005) [Pubmed]
  14. Polyphosphate loss promotes SNF/SWI- and Gcn5-dependent mitotic induction of PHO5. Neef, D.W., Kladde, M.P. Mol. Cell. Biol. (2003) [Pubmed]
  15. The yeast acid phosphatase can enter the secretory pathway without its N-terminal signal sequence. Silve, S., Monod, M., Hinnen, A., Haguenauer-Tsapis, R. Mol. Cell. Biol. (1987) [Pubmed]
  16. In vitro assembly of the characteristic chromatin organization at the yeast PHO5 promoter by a replication-independent extract system. Korber, P., Hörz, W. J. Biol. Chem. (2004) [Pubmed]
  17. Expression, glycosylation and secretion of yeast acid phosphatase in hamster BHK cells. Reljic, R., Barbaric, S., Ries, B., Buxton, R., Hughes, R.C. Glycoconj. J. (1992) [Pubmed]
  18. Phosphate transport and sensing in Saccharomyces cerevisiae. Wykoff, D.D., O'Shea, E.K. Genetics (2001) [Pubmed]
  19. Depletion of histone H4 and nucleosomes activates the PHO5 gene in Saccharomyces cerevisiae. Han, M., Kim, U.J., Kayne, P., Grunstein, M. EMBO J. (1988) [Pubmed]
  20. Isolation and characterization of mutations affecting expression of the delta9- fatty acid desaturase gene, OLE1, in Saccharomyces cerevisiae. Fujimori, K., Anamnart, S., Nakagawa, Y., Sugioka, S., Ohta, D., Oshima, Y., Yamada, Y., Harashima, S. FEBS Lett. (1997) [Pubmed]
  21. The yeast PHO5 promoter: phosphate-control elements and sequences mediating mRNA start-site selection. Rudolph, H., Hinnen, A. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  22. 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]
  23. Elevated expression of stress response genes resulting from deletion of the PHO85 gene. Timblin, B.K., Bergman, L.W. Mol. Microbiol. (1997) [Pubmed]
  24. Transcriptional regulation of the yeast PHO8 promoter in comparison to the coregulated PHO5 promoter. Munsterkötter, M., Barbaric, S., Hörz, W. J. Biol. Chem. (2000) [Pubmed]
  25. Increase in gene expression by respiratory-deficient mutation. Kaisho, Y., Yoshimura, K., Nakahama, K. Yeast (1989) [Pubmed]
  26. Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast. Gregory, P.D., Schmid, A., Zavari, M., Lui, L., Berger, S.L., Hörz, W. Mol. Cell (1998) [Pubmed]
  27. The transactivation domain of Pho4 is required for nucleosome disruption at the PHO5 promoter. Svaren, J., Schmitz, J., Hörz, W. EMBO J. (1994) [Pubmed]
  28. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Rundlett, S.E., Carmen, A.A., Kobayashi, R., Bavykin, S., Turner, B.M., Grunstein, M. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  29. Multiple mechanistically distinct functions of SAGA at the PHO5 promoter. Barbaric, S., Reinke, H., Hörz, W. Mol. Cell. Biol. (2003) [Pubmed]
  30. 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]
  31. Redundancy of chromatin remodeling pathways for the induction of the yeast PHO5 promoter in vivo. Barbaric, S., Luckenbach, T., Schmid, A., Blaschke, D., Hörz, W., Korber, P. J. Biol. Chem. (2007) [Pubmed]
  32. 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]
  33. Biochemical properties and excretion behavior of repressible acid phosphatases with altered subunit composition. Shnyreva, M.G., Petrova, E.V., Egorov, S.N., Hinnen, A. Microbiol. Res. (1996) [Pubmed]
 
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