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Gene Review

PGK1  -  phosphoglycerate kinase

Saccharomyces cerevisiae S288c

Synonyms: Phosphoglycerate kinase, YCR012W, YCR12W
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Disease relevance of PGK1


High impact information on PGK1

  • Space-filling models of yeast hexokinase, adenylate kinase, and phosphoglycerate kinase drawn by computer clearly portray the bilobal character of these phosphoryl transfer enzymes, and the deep cleft which is formed between the lobes [5].
  • Regardless of the position of an amber codon in the PGK1 gene, deletion of the UPF1 gene restores wild-type decay rates to nonsense-containing PGK1 transcripts [6].
  • In addition, using hybrid GCN4-PGK1 transcripts, we demonstrate that if a translational reinitiation signal precedes a downstream element, the mRNA will no longer be sensitive to nonsense-mediated decay [7].
  • Immunoelectron microscopy showed that two cytosolic marker enzymes, alcohol dehydrogenase and phosphoglycerate kinase, are present in the autophagic bodies at the same densities as in the cytosol, but are not present in vacuolar sap, suggesting that cytosolic enzymes are also taken up into the autophagic bodies [8].
  • This gene which is under the control of the Saccharomyces cerevisiae phosphoglycerate kinase promoter is integrated in a chromosome different from the one containing the endogenous gene [9].

Chemical compound and disease context of PGK1


Biological context of PGK1

  • To understand the RNA structural features that dictate mRNA decay rates in yeast, we have constructed PGK1/MAT alpha 1 and ACT1/MAT alpha 1 gene fusions and analyzed the decay rates of the resultant chimeric transcripts [10].
  • As an experimental approach to studying biased codon usage and its possible role in modulating gene expression, systematic codon replacements were carried out in the highly expressed PGK1 gene [11].
  • The frequency of meiotic crossing over in the CEN3-PGK1 and LEU2-CEN3 intervals increases approximately 1.5- and fourfold, respectively, when CEN3 is repositioned at HIS4 [12].
  • This short form of hexokinase II was produced from a fusion between the promoter region of the PGK1 gene and the HXK2 coding sequence except the first 15 codons [13].
  • The PGK1 gene can be applied as a direct positive selection marker to obtain a high episomal plasmid stability during growth on glucose [14].

Anatomical context of PGK1


Associations of PGK1 with chemical compounds


Physical interactions of PGK1


Regulatory relationships of PGK1

  • This suggests that RAP1 may be involved in transcriptional control of many other glycolytic genes in addition to the PGK gene [21].
  • Mutants carrying fusions to an enhancer-less version of the PGK1 promoter (PGK1(Delta767)) expressed Pyk1 and Pf1k at about 2.5-fold lower levels than normal [28].
  • The highest XR or XDH activities were obtained when the expressed gene was controlled by the PGK promoter and located downstream after the ADHI promoter-gene-terminator sequence [29].
  • Translation of two-thirds of the PGK1 coding region inactivates the nonsense-mediated mRNA decay pathway [30].
  • Furthermore, we find that Gcr1p positively influences PGK transcription, although it is not responsible for the carbon source dependent regulation of PGK mRNA synthesis [25].

Other interactions of PGK1

  • Transcriptional control of the Saccharomyces cerevisiae PGK gene by RAP1 [21].
  • Characterization of the decay of nonsense-containing HIS4 transcripts yielded results mirroring those described above, suggesting that the sequence requirements described for the PGK1 transcript are likely to be a general characteristic of this decay pathway [30].
  • The organisation of the PGK and PYK1 UASs is thus similar to each other and to the transcriptional silencer HMR(E) which also contains these sequences [31].
  • Surprisingly, the STE3 3' UT is not sufficient to accelerate the turnover of the stable PGK1 transcript unless portions of the PGK1 coding region are first deleted [32].
  • The cis acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon [33].

Analytical, diagnostic and therapeutic context of PGK1


  1. Ethanolic fermentation of xylose with Saccharomyces cerevisiae harboring the Thermus thermophilus xylA gene, which expresses an active xylose (glucose) isomerase. Walfridsson, M., Bao, X., Anderlund, M., Lilius, G., Bülow, L., Hahn-Hägerdal, B. Appl. Environ. Microbiol. (1996) [Pubmed]
  2. Isolation and characterization of the yeast 3-phosphoglycerokinase gene (PGK) by an immunological screening technique. Hitzeman, R.A., Clarke, L., Carbon, J. J. Biol. Chem. (1980) [Pubmed]
  3. The structure of a thermally stable 3-phosphoglycerate kinase and a comparison with its mesophilic equivalent. Davies, G.J., Gamblin, S.J., Littlechild, J.A., Watson, H.C. Proteins (1993) [Pubmed]
  4. Effect of Cibacron Blue F3GA on phosphoglycerate kinase of Lactobacillus plantarum and phosphoglycerate mutase of Leuconostoc dextranicum. Kawai, K., Eguchi, Y. J. Biochem. (1980) [Pubmed]
  5. Space-filling models of kinase clefts and conformation changes. Anderson, C.M., Zucker, F.H., Steitz, T.A. Science (1979) [Pubmed]
  6. mRNA destabilization triggered by premature translational termination depends on at least three cis-acting sequence elements and one trans-acting factor. Peltz, S.W., Brown, A.H., Jacobson, A. Genes Dev. (1993) [Pubmed]
  7. Utilizing the GCN4 leader region to investigate the role of the sequence determinants in nonsense-mediated mRNA decay. Ruiz-Echevarria, M.J., Peltz, S.W. EMBO J. (1996) [Pubmed]
  8. Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization. Baba, M., Takeshige, K., Baba, N., Ohsumi, Y. J. Cell Biol. (1994) [Pubmed]
  9. Alcohol oxidase expressed under nonmethylotrophic conditions is imported, assembled, and enzymatically active in peroxisomes of Hansenula polymorpha. Distel, B., Van der Leÿ, I., Veenhuis, M., Tabak, H.F. J. Cell Biol. (1988) [Pubmed]
  10. Translation and a 42-nucleotide segment within the coding region of the mRNA encoded by the MAT alpha 1 gene are involved in promoting rapid mRNA decay in yeast. Parker, R., Jacobson, A. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  11. Codon replacement in the PGK1 gene of Saccharomyces cerevisiae: experimental approach to study the role of biased codon usage in gene expression. Hoekema, A., Kastelein, R.A., Vasser, M., de Boer, H.A. Mol. Cell. Biol. (1987) [Pubmed]
  12. Repression of meiotic crossing over by a centromere (CEN3) in Saccharomyces cerevisiae. Lambie, E.J., Roeder, G.S. Genetics (1986) [Pubmed]
  13. The 15 N-terminal amino acids of hexokinase II are not required for in vivo function: analysis of a truncated form of hexokinase II in Saccharomyces cerevisiae. Ma, H., Bloom, L.M., Dakin, S.E., Walsh, C.T., Botstein, D. Proteins (1989) [Pubmed]
  14. Effects of phosphoglycerate kinase overproduction in Saccharomyces cerevisiae on the physiology and plasmid stability. van der Aar, P.C., van den Heuvel, J.J., Röling, W.F., Raué, H.A., Stouthamer, A.H., van Verseveld, H.W. Yeast (1992) [Pubmed]
  15. Turnover mechanisms of the stable yeast PGK1 mRNA. Muhlrad, D., Decker, C.J., Parker, R. Mol. Cell. Biol. (1995) [Pubmed]
  16. The complete amino acid sequence of yeast phosphoglycerate kinase. Perkins, R.E., Conroy, S.C., Dunbar, B., Fothergill, L.A., Tuite, M.F., Dobson, M.J., Kingsman, S.M., Kingsman, A.J. Biochem. J. (1983) [Pubmed]
  17. 3-phosphoglycerate kinase: a glycolytic enzyme protein present in the cell wall of Candida albicans. Alloush, H.M., López-Ribot, J.L., Masten, B.J., Chaffin, W.L. Microbiology (Reading, Engl.) (1997) [Pubmed]
  18. Binding of glycolytic enzymes to cardiac sarcolemmal and sarcoplasmic reticular membranes. Pierce, G.N., Philipson, K.D. J. Biol. Chem. (1985) [Pubmed]
  19. Calmodulin binds to and inhibits the activity of phosphoglycerate kinase. Myre, M.A., O'Day, D.H. Biochim. Biophys. Acta (2004) [Pubmed]
  20. Engineering of an oenological Saccharomyces cerevisiae strain with pectinolytic activity and its effect on wine. Fernández-González, M., Ubeda, J.F., Cordero-Otero, R.R., Thanvanthri Gururajan, V., Briones, A.I. Int. J. Food Microbiol. (2005) [Pubmed]
  21. Transcriptional control of the Saccharomyces cerevisiae PGK gene by RAP1. Chambers, A., Tsang, J.S., Stanway, C., Kingsman, A.J., Kingsman, S.M. Mol. Cell. Biol. (1989) [Pubmed]
  22. Genetic perturbation of glycolysis results in inhibition of de novo inositol biosynthesis. Shi, Y., Vaden, D.L., Ju, S., Ding, D., Geiger, J.H., Greenberg, M.L. J. Biol. Chem. (2005) [Pubmed]
  23. Overproduction of pentose phosphate pathway enzymes using a new CRE-loxP expression vector for repeated genomic integration in Saccharomyces cerevisiae. Johansson, B., Hahn-Hägerdal, B. Yeast (2002) [Pubmed]
  24. Linking mRNA turnover and translation: assessing the polyribosomal association of mRNA decay factors and degradative intermediates. Mangus, D.A., Jacobson, A. Methods (1999) [Pubmed]
  25. The yeast protein Gcr1p binds to the PGK UAS and contributes to the activation of transcription of the PGK gene. Henry, Y.A., López, M.C., Gibbs, J.M., Chambers, A., Kingsman, S.M., Baker, H.V., Stanway, C.A. Mol. Gen. Genet. (1994) [Pubmed]
  26. Immobilized glyceraldehyde-3-phosphate dehydrogenase forms a complex with phosphoglycerate kinase. Ashmarina, L.I., Muronetz, V.I., Nagradova, N.K. Biochem. Int. (1984) [Pubmed]
  27. Phosphorylation influences the binding of the yeast RAP1 protein to the upstream activating sequence of the PGK gene. Tsang, J.S., Henry, Y.A., Chambers, A., Kingsman, A.J., Kingsman, S.M. Nucleic Acids Res. (1990) [Pubmed]
  28. Pyruvate kinase (Pyk1) levels influence both the rate and direction of carbon flux in yeast under fermentative conditions. Pearce, A.K., Crimmins, K., Groussac, E., Hewlins, M.J., Dickinson, J.R., Francois, J., Booth, I.R., Brown, A.J. Microbiology (Reading, Engl.) (2001) [Pubmed]
  29. Effect on product formation in recombinant Saccharomyces cerevisiae strains expressing different levels of xylose metabolic genes. Bao, X., Gao, D., Qu, Y., Wang, Z., Walfridssion, M., Hahn-Hagerbal, B. Chin. J. Biotechnol. (1997) [Pubmed]
  30. Characterization of cis-acting sequences and decay intermediates involved in nonsense-mediated mRNA turnover. Hagan, K.W., Ruiz-Echevarria, M.J., Quan, Y., Peltz, S.W. Mol. Cell. Biol. (1995) [Pubmed]
  31. ARS binding factor 1 binds adjacent to RAP1 at the UASs of the yeast glycolytic genes PGK and PYK1. Chambers, A., Stanway, C., Tsang, J.S., Henry, Y., Kingsman, A.J., Kingsman, S.M. Nucleic Acids Res. (1990) [Pubmed]
  32. Analysis of chimeric mRNAs derived from the STE3 mRNA identifies multiple regions within yeast mRNAs that modulate mRNA decay. Heaton, B., Decker, C., Muhlrad, D., Donahue, J., Jacobson, A., Parker, R. Nucleic Acids Res. (1992) [Pubmed]
  33. The cis acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon. LaGrandeur, T., Parker, R. RNA (1999) [Pubmed]
  34. The gcr (glycolysis regulation) mutation of Saccharomyces cerevisiae. Clifton, D., Fraenkel, D.G. J. Biol. Chem. (1981) [Pubmed]
  35. The multifunctional transcription factors Abf1p, Rap1p and Reb1p are required for full transcriptional activation of the chromosomal PGK gene in Saccharomyces cerevisiae. Packham, E.A., Graham, I.R., Chambers, A. Mol. Gen. Genet. (1996) [Pubmed]
  36. Xylitol production by recombinant Saccharomyces cerevisiae expressing the Pichia stipitis and Candida shehatae XYL1 genes. Govinden, R., Pillay, B., van Zyl, W.H., Pillay, D. Appl. Microbiol. Biotechnol. (2001) [Pubmed]
  37. Molecular characterization of the 3-phosphoglycerate kinase gene (PGK1) from the methylotrophic yeast Pichia pastoris. de Almeida, J.R., de Moraes, L.M., Torres, F.A. Yeast (2005) [Pubmed]
  38. Chemical modification of yeast 3-phosphoglycerate kinase. Markland, F.S., Bacharach, A.D., Weber, B.H., O'Grady, T.C., Saunders, G.C., Umemura, N. J. Biol. Chem. (1975) [Pubmed]
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