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Gene Review

HYR1  -  peroxiredoxin HYR1

Saccharomyces cerevisiae S288c

Synonyms: GPX3, Glutathione peroxidase 3, Hydrogen peroxide resistance protein 1, ORP1, Oxidant receptor peroxidase 1, ...
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Disease relevance of HYR1


High impact information on HYR1


Chemical compound and disease context of HYR1

  • Using the comparison between cGpx3 and Gpx3 in conjunction with other constructs to probe lipid peroxidation as a toxicity mechanism, we also ascertained that lipid peroxidation-dependent processes are a principal cause of cellular cadmium toxicity [4].

Biological context of HYR1

  • The results show that the GPX genes of S. cerevisiae, previously reported to encode GPxs, encode PHGPxs (PHGPx1, PHGPx2, and PHGPx3) and that these enzymes protect yeast against phospholipid hydroperoxides as well as nonphospholipid peroxides during oxidative stress [1].
  • Gpx3 is a ubiquitously expressed isoform that modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathways and protein translocation [5].
  • The Gpx3 (Orp1/PHGpx3) protein transduces the hydroperoxide signal to the transcription factor Yap1, a function that could account for most GPX-dependent phenotypes [4].
  • Orp1p is found in the nucleus and is present at a constant level throughout the cell cycle [3].
  • The orp1 gene is also required for the control that prevents entry into mitosis in the absence of DNA replication, suggesting a role for ORC in this checkpoint pathway [3].

Anatomical context of HYR1

  • RECENT FINDINGS: The long variant of ORP1 is induced upon differentiation of monocytes to macrophages and has capacity to enhance the trans-activation potential of liver X receptors, indicating a function in macrophage lipid metabolism [6].

Associations of HYR1 with chemical compounds


Other interactions of HYR1

  • The GPX1, GPX2, and GPX3 genes of Saccharomyces cerevisiae have been reported previously to encode glutathione peroxidases (GPxs) [1].
  • We show here that the requirement for Gpx3 in the regulation of Yap1 is strain-specific [12].
  • Sequencing of the HYR-mediating passenger DNA revealed that SNG1 encodes a 547 a polypeptide containing seven transmembrane-spanning regions that may be membrane-bound [13].

Analytical, diagnostic and therapeutic context of HYR1

  • In order to search for the interaction partners of Gpx3, we carried out immunoprecipitation/2-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay [5].
  • Genetic dissection of the phospholipid hydroperoxidase activity of yeast gpx3 reveals its functional importance [4].
  • Both gel-filtration and dynamic light-scattering (DLS) results indicate that Gpx3 is a monomer in solution at a concentration of about 2 mg ml(-1), whereas glutathione peroxidases are normally tetrameric or dimeric [14].
  • A chromatin immunoprecipitation assay demonstrated that Orp1p was preferentially localized at the ars2004 and ars3002 origins of the chromosome throughout the cell cycle, while SpMcm6p was associated with these origins only in the G(1) and S phases [15].


  1. Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases. Avery, A.M., Avery, S.V. J. Biol. Chem. (2001) [Pubmed]
  2. A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation. Delaunay, A., Pflieger, D., Barrault, M.B., Vinh, J., Toledano, M.B. Cell (2002) [Pubmed]
  3. The ORC1 homolog orp1 in fission yeast plays a key role in regulating onset of S phase. Grallert, B., Nurse, P. Genes Dev. (1996) [Pubmed]
  4. Genetic dissection of the phospholipid hydroperoxidase activity of yeast gpx3 reveals its functional importance. Avery, A.M., Willetts, S.A., Avery, S.V. J. Biol. Chem. (2004) [Pubmed]
  5. Glutathione peroxidase 3 of Saccharomyces cerevisiae regulates the activity of methionine sulfoxide reductase in a redox state-dependent way. Kho, C.W., Lee, P.Y., Bae, K.H., Cho, S., Lee, Z.W., Park, B.C., Kang, S., Lee, d.o. .H., Park, S.G. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  6. Oxysterol binding protein and its homologues: new regulatory factors involved in lipid metabolism. Olkkonen, V.M. Curr. Opin. Lipidol. (2004) [Pubmed]
  7. Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae. Inoue, Y., Matsuda, T., Sugiyama, K., Izawa, S., Kimura, A. J. Biol. Chem. (1999) [Pubmed]
  8. Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor. Veal, E.A., Ross, S.J., Malakasi, P., Peacock, E., Morgan, B.A. J. Biol. Chem. (2003) [Pubmed]
  9. Thermodynamic basis for redox regulation of the yap1 signal transduction pathway. Mason, J.T., Kim, S.K., Knaff, D.B., Wood, M.J. Biochemistry (2006) [Pubmed]
  10. Low glutathione pools in the original pso3 mutant of Saccharomyces cerevisiae are responsible for its pleiotropic sensitivity phenotype. Brendel, M., Grey, M., Maris, A.F., Hietkamp, J., Fesus, Z., Pich, C.T., Dafré, A.L., Schmidt, M., Eckardt-Schupp, F., Henriques, J.A. Curr. Genet. (1998) [Pubmed]
  11. Molecular mechanism of oxidative stress perception by the Orp1 protein. Ma, L.H., Takanishi, C.L., Wood, M.J. J. Biol. Chem. (2007) [Pubmed]
  12. Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast. Okazaki, S., Naganuma, A., Kuge, S. Antioxid. Redox Signal. (2005) [Pubmed]
  13. SNG1--a new gene involved in nitrosoguanidine resistance in Saccharomyces cerevisiae. Grey, M., Pich, C.T., Haase, E., Brendel, M. Mutat. Res. (1995) [Pubmed]
  14. Purification, crystallization and preliminary X-ray analysis of glutathione peroxidase Gpx3 from Saccharomyces cerevisiae. Yang, Z., Zhou, C.Z. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  15. Association of fission yeast Orp1 and Mcm6 proteins with chromosomal replication origins. Ogawa, Y., Takahashi, T., Masukata, H. Mol. Cell. Biol. (1999) [Pubmed]
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