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Gene Review

GRX1  -  dithiol glutaredoxin GRX1

Saccharomyces cerevisiae S288c

Synonyms: Glutaredoxin-1, Glutathione-dependent oxidoreductase 1, YCL035C, YCL35C
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Disease relevance of GRX1

  • The results demonstrate a novel hydrogen transport system in E. coli consisting of NADPH, glutathione, glutathione reductase, and a heat-stable enzyme called "glutaredoxin". Reduced glutathione at physiological concentrations functions as hydrogen donor for ribonucleotide reduction only in the presence of glutaredoxin [1].

High impact information on GRX1

  • In contrast, depletion of the Hsp70 chaperone Ssq1p, its co-chaperone Jac1p or the glutaredoxin Grx5p markedly increased the amount of Fe/S clusters bound to Isu1p, even though these mitochondrial proteins are crucial for maturation of Fe/S proteins [2].
  • 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 [3].
  • In this work, another subfamily of yeast glutaredoxins (Grx3, Grx4, and Grx5) that differs from the first in containing a single cysteine residue at the putative active site is described [3].
  • Mutants lacking Grx5 are partially deficient in growth in rich and minimal media and also highly sensitive to oxidative damage caused by menadione and hydrogen peroxide [3].
  • The interaction between glutaredoxins and Aft1 is not modulated by the iron status of cells but is dependent on the conserved glutaredoxin domain Cys residue [4].

Biological context of GRX1


Associations of GRX1 with chemical compounds

  • The yeast Saccharomyces cerevisiae contains two glutaredoxins, encoded by GRX1 and GRX2, which are active as glutathione-dependent oxidoreductases [5].
  • 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 [6].
  • 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 [7].
  • Thus yeast glutaredoxin is unable to substitute for thioredoxin in sulfate assimilation [10].
  • However, during oxidation by H(2)O(2), hydroxyethyl disulfide, or cystine, the glutaredoxin domain reacted first, followed by a rate-limiting (0.13 min(-)(1)) transfer of a disulfide bond to the other domain [11].

Regulatory relationships of GRX1

  • GRX1 contains a single STRE element and is induced to significantly higher levels compared to GRX2 following heat and osmotic shock [12].

Other interactions of GRX1

  • A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae [13].
  • We recently reported that Grx1 is active as a glutathione peroxidase and can directly reduce hydroperoxides (Collinson, E. J., Wheeler, G. L., Garrido, E. O., Avery, A. M., Avery, S. V., and Grant, C. M. (2002) J. Biol. Chem. 277, 16712-16717) [6].
  • These data suggest that Ure2 possesses a central role in metal ion detoxification, a role not demonstrably shared by either of the two known S. cerevisiae glutathione S-transferases, Gtt1 and Gtt2, or the two glutaredoxins, Grx1 and Grx2, that also possess glutathione S-transferase activity [14].
  • This suggests that during the catalytic cycle, Acr2p forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active Acr2p reductase [15].
  • Yeast Grx5 is the only glutaredoxin-like protein studied biochemically so far [16].

Analytical, diagnostic and therapeutic context of GRX1


  1. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Holmgren, A. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  2. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. Mühlenhoff, U., Gerber, J., Richhardt, N., Lill, R. EMBO J. (2003) [Pubmed]
  3. 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]
  4. Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae. Ojeda, L., Keller, G., Muhlenhoff, U., Rutherford, J.C., Lill, R., Winge, D.R. J. Biol. Chem. (2006) [Pubmed]
  5. 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]
  6. Role of yeast glutaredoxins as glutathione S-transferases. Collinson, E.J., Grant, C.M. J. Biol. Chem. (2003) [Pubmed]
  7. 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]
  8. Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Grant, C.M. Mol. Microbiol. (2001) [Pubmed]
  9. Arsenate reduction: thiol cascade chemistry with convergent evolution. Messens, J., Silver, S. J. Mol. Biol. (2006) [Pubmed]
  10. Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. Muller, E.G. J. Biol. Chem. (1991) [Pubmed]
  11. Mechanistic insight provided by glutaredoxin within a fusion to redox-sensitive yellow fluorescent protein. Björnberg, O., Østergaard, H., Winther, J.R. Biochemistry (2006) [Pubmed]
  12. 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]
  13. A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae. Draculic, T., Dawes, I.W., Grant, C.M. Mol. Microbiol. (2000) [Pubmed]
  14. In vivo specificity of Ure2 protection from heavy metal ion and oxidative cellular damage in Saccharomyces cerevisiae. Rai, R., Cooper, T.G. Yeast (2005) [Pubmed]
  15. Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase. Mukhopadhyay, R., Shi, J., Rosen, B.P. J. Biol. Chem. (2000) [Pubmed]
  16. Plasmodium falciparum glutaredoxin-like proteins. Deponte, M., Becker, K., Rahlfs, S. Biol. Chem. (2005) [Pubmed]
  17. Characterization of mammalian thioredoxin reductase, thioredoxin and glutaredoxin by immunochemical methods. Martínez-Galisteo, E., Padilla, C.A., Holmgren, A., Bárcena, J.A. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1995) [Pubmed]
  18. Crystallization of mutant forms of glutaredoxin Grx1p from yeast. Håkansson, K.O., Østergaard, H., Winther, J.R. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
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