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PPN1  -  Ppn1p

Saccharomyces cerevisiae S288c

Synonyms: D9461.37, Endopolyphosphatase, Exopolyphosphatase, PHM5, Phosphate metabolism protein 5, ...
 
 
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Disease relevance of PPN1

  • The effect of PPN1 inactivation on the polyP level in the nuclei is insignificant in the stationary phase, while in the exponential phase this level increases 2.3-fold as compared with the parent strain of S. cerevisiae [1].
 

High impact information on PPN1

  • Here we show that Bsd2 provides an alternative ubiquitination mechanism for Cps1, Phm5 and other proteins [2].
  • Mutation of Lys 6 in the cytoplasmic tail of Phm5p disrupts its sorting, but sorting is restored, even in doa4 cells, by the biosynthetic addition of a single ubiquitin chain [3].
  • A double mutant of PPN1 and PPX1 (the gene encoding a potent exopolyphosphatase) loses viability rapidly in stationary phase [4].
  • That PPN1 encodes Ppn1 was verified by a 25-fold increase in Ppn1 when overexpressed under a GAL promoter and also by several peptide sequences that match exactly with sequences in a yeast genome ORF, the mutation of which abolishes Ppn1 activity [4].
  • Yeast exopolyphosphatase (scPPX) processively splits off the terminal phosphate group from linear polyphosphates longer than pyrophosphate. scPPX belongs to the DHH phosphoesterase superfamily and is evolutionarily close to the well characterized family II pyrophosphatase (PPase) [5].
 

Biological context of PPN1

 

Anatomical context of PPN1

  • Inactivation of PPN1 decreased the polyphosphate level in the cytosol 1.4-fold and increased it 2- and 2.5-fold in mitochondria and vacuoles, respectively [7].
  • Effects of inactivation of the PPN1 gene on exopolyphosphatases, inorganic polyphosphates and function of mitochondria in the yeast Saccharomyces cerevisiae [8].
  • We also show that, like fab1Delta mutants, vac14Delta cells fail to sort GFP-Phm5 to the MVB and thence to the vacuole: irreversible ubiquitination of GFP-Phm5 overcomes this defect [9].
  • Precursor forms of vacuolar proteins with transmembrane domains, such as the carboxypeptidase S Cps1p and the polyphosphatase Phm5p, are selectively sorted in endosomal compartments to vesicles that invaginate, budding into the lumen of the late endosomes, resulting in the formation of multivesicular bodies (MVBs) [10].
  • Osteoblast-like cell exopolyphosphatase activity and exopolyphosphatase activity in yeast, rat tissues, and human leukemia cell line HL60 were inhibited by the bisphosphonates etidronate and, to a lesser extent, clodronate and pamidronate [11].
 

Associations of PPN1 with chemical compounds

  • The average chain length of mitochondrial polyphosphates at the stationary growth stage on glucose was about 15-20 and about 130-180 phosphate residues in the parent strain and PPN1 mutants, respectively [8].
  • Mutants of Saccharomyces cerevisiae with inactivated endopolyphosphatase gene PPN1 did not grow on lactate and ethanol, and stopped growth on glucose earlier than the parent strain [8].
  • Unlike the enzyme encoded by PPX1, the high-molecular-mass exopolyphosphatase is slightly active with polyP3, not inhibited by antibodies suppressing the activity of 40-kD exopolyphosphatase, inhibited by EDTA, and stimulated by divalent cations to a lesser extent [12].
  • The decrease in polyphosphate content during treatment with dexamethasone, beta-glycerophosphate, epidermal growth factor, and ascorbic acid was accompanied by a decrease in exopolyphosphatase, pyrophosphatase, and alkaline phosphatase activity [11].
  • Adenosine 5'-tetraphosphate phosphohydrolase activity is an inherent property of soluble exopolyphosphatase from yeast Saccharomyces cerevisiae [13].
 

Other interactions of PPN1

  • Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes [7].

References

  1. Inorganic polyphosphate and exopolyphosphatase in the nuclei of Saccharomyces cerevisiae: dependence on the growth phase and inactivation of the PPX1 and PPN1 genes. Lichko, L.P., Kulakovskaya, T.V., Kulaev, I.S. Yeast (2006) [Pubmed]
  2. Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. Hettema, E.H., Valdez-Taubas, J., Pelham, H.R. EMBO J. (2004) [Pubmed]
  3. Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting. Reggiori, F., Pelham, H.R. EMBO J. (2001) [Pubmed]
  4. The endopolyphosphatase gene: essential in Saccharomyces cerevisiae. Sethuraman, A., Rao, N.N., Kornberg, A. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  5. Kinetic and Mutational Analyses of the Major Cytosolic Exopolyphosphatase from Saccharomyces cerevisiae. Tammenkoski, M., Moiseev, V.M., Lahti, M., Ugochukwu, E., Brondijk, T.H., White, S.A., Lahti, R., Baykov, A.A. J. Biol. Chem. (2007) [Pubmed]
  6. New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis. Ogawa, N., DeRisi, J., Brown, P.O. Mol. Biol. Cell (2000) [Pubmed]
  7. Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes. Lichko, L., Kulakovskaya, T., Pestov, N., Kulaev, I. Biosci. Rep. (2006) [Pubmed]
  8. Effects of inactivation of the PPN1 gene on exopolyphosphatases, inorganic polyphosphates and function of mitochondria in the yeast Saccharomyces cerevisiae. Pestov, N.A., Kulakovskaya, T.V., Kulaev, I.S. FEMS Yeast Res. (2005) [Pubmed]
  9. Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body. Dove, S.K., McEwen, R.K., Mayes, A., Hughes, D.C., Beggs, J.D., Michell, R.H. Curr. Biol. (2002) [Pubmed]
  10. The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies. Morvan, J., Froissard, M., Haguenauer-Tsapis, R., Urban-Grimal, D. Traffic (2004) [Pubmed]
  11. Inorganic polyphosphate in human osteoblast-like cells. Leyhausen, G., Lorenz, B., Zhu, H., Geurtsen, W., Bohnensack, R., Müller, W.E., Schröder, H.C. J. Bone Miner. Res. (1998) [Pubmed]
  12. Purification and properties of exopolyphosphatase from the cytosol of Saccharomyces cerevisiae not encoded by the PPX1 gene. Andreeva, N.A., Kulakovskaya, T.V., Kulaev, I.S. Biochemistry Mosc. (2004) [Pubmed]
  13. Adenosine 5'-tetraphosphate phosphohydrolase activity is an inherent property of soluble exopolyphosphatase from yeast Saccharomyces cerevisiae. Guranowski, A., Starzyńska, E., Barnes, L.D., Robinson, A.K., Liu, S. Biochim. Biophys. Acta (1998) [Pubmed]
 
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