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Gene Review

GRX2  -  dithiol glutaredoxin GRX2

Saccharomyces cerevisiae S288c

Synonyms: D9719.17, Glutaredoxin-2, mitochondrial, Glutathione-dependent oxidoreductase 2, TTR, TTR1, ...
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Disease relevance of GRX2


High impact information on GRX2

  • In Saccharomyces cerevisiae, two glutaredoxins (Grx1 and Grx2) containing a cysteine pair at the active site had been characterized as protecting yeast cells against oxidative damage [2].
  • The product of the yeast GRX2 gene is a protein that is localized both in the cytosol and mitochondria [3].
  • The mitochondrial targeting properties of the presequence and the influence of the mature part of Grx2 were analyzed by the characterization of the import kinetics of specific fusion proteins [3].
  • Our results show that a plethora of Grx2 subcellular localizations could spread its antioxidant functions all over the cell, but one single Ala to Gly mutation converts Grx2 into a typical protein of the mitochondrial matrix [3].
  • We have addressed the functional divergence among glutaredoxins by targeting Grx2/3/4 molecules to the mitochondrial matrix using the Grx5 targeting sequence [4].

Chemical compound and disease context of GRX2


Biological context of GRX2


Associations of GRX2 with chemical compounds

  • Thus, Grx1 and Grx2 function differently in the cell, and we suggest that glutaredoxins may act as one of the primary defenses against mixed disulfides formed following oxidative damage to proteins [6].
  • The yeast Saccharomyces cerevisiae contains two glutaredoxins, encoded by GRX1 and GRX2, which are active as glutathione-dependent oxidoreductases [7].
  • We now show that Grx2 is also a general hydroperoxidase, and kinetic data indicate that both enzymes have a similar pattern of activity, which is highest with hydrogen peroxide, followed by cumene hydroperoxide and tert-butyl hydroperoxide [9].
  • Furthermore, both Grx1 and Grx2 are shown be active as glutathione S-transferases (GSTs), and their activity with model substrates such as 1-chloro-2,4-dinitrobenzene is similar to their activity with hydroperoxides [9].
  • The variation pattern of the level of hydroxyl-radical adducts correlated with the one determined for the activity of Sod1p, cytosolic catalase Ctt1p, and the dithiol glutaredoxins Grx1p and Grx2p [10].

Regulatory relationships of GRX2

  • GRX1 contains a single STRE element and is induced to significantly higher levels compared to GRX2 following heat and osmotic shock [11].

Other interactions of GRX2


Analytical, diagnostic and therapeutic context of GRX2


  1. A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase. Fernandes, A.P., Fladvad, M., Berndt, C., Andrésen, C., Lillig, C.H., Neubauer, P., Sunnerhagen, M., Holmgren, A., Vlamis-Gardikas, A. J. Biol. Chem. (2005) [Pubmed]
  2. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Rodríguez-Manzaneque, M.T., Ros, J., Cabiscol, E., Sorribas, A., Herrero, E. Mol. Cell. Biol. (1999) [Pubmed]
  3. One single in-frame AUG codon is responsible for a diversity of subcellular localizations of glutaredoxin 2 in Saccharomyces cerevisiae. Porras, P., Padilla, C.A., Krayl, M., Voos, W., Bárcena, J.A. J. Biol. Chem. (2006) [Pubmed]
  4. Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins. Molina, M.M., Bellí, G., de la Torre, M.A., Rodríguez-Manzaneque, M.T., Herrero, E. J. Biol. Chem. (2004) [Pubmed]
  5. Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments. Pedrajas, J.R., Porras, P., Martínez-Galisteo, E., Padilla, C.A., Miranda-Vizuete, A., Bárcena, J.A. Biochem. J. (2002) [Pubmed]
  6. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Luikenhuis, S., Perrone, G., Dawes, I.W., Grant, C.M. Mol. Biol. Cell (1998) [Pubmed]
  7. The yeast glutaredoxins are active as glutathione peroxidases. Collinson, E.J., Wheeler, G.L., Garrido, E.O., Avery, A.M., Avery, S.V., Grant, C.M. J. Biol. Chem. (2002) [Pubmed]
  8. Complete amino acid sequence of yeast thioltransferase (glutaredoxin). Gan, Z.R., Polokoff, M.A., Jacobs, J.W., Sardana, M.K. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  9. Role of yeast glutaredoxins as glutathione S-transferases. Collinson, E.J., Grant, C.M. J. Biol. Chem. (2003) [Pubmed]
  10. The herbicide 2,4-dichlorophenoxyacetic acid induces the generation of free-radicals and associated oxidative stress responses in yeast. Teixeira, M.C., Telo, J.P., Duarte, N.F., Sá-Correia, I. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  11. Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae. Grant, C.M., Luikenhuis, S., Beckhouse, A., Soderbergh, M., Dawes, I.W. Biochim. Biophys. Acta (2000) [Pubmed]
  12. Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe. Chung, W.H., Kim, K.D., Roe, J.H. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  13. Cloning and sequencing of a gene encoding yeast thioltransferase. Gan, Z.R. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
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