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Gene Review

GRX4  -  monothiol glutaredoxin GRX4

Saccharomyces cerevisiae S288c

Synonyms: Monothiol glutaredoxin-4, SYGP-ORF64, YER174C
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Disease relevance of GRX4


High impact information on GRX4

  • 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 [2].
  • Thus, Grx3 and Grx4 are novel components required for Aft1 iron regulation that most likely occurs in the nucleus [3].
  • Grx3 and Grx4 interact with Aft1 as shown by two-hybrid interactions and co-immunoprecipitation assays [3].
  • Experiments with gene knock-out techniques showed that the reading frame encoding Grx4 was essential [1].
  • Grx4 in reduced form contained three thiols, and treatment with oxidized GSH resulted in glutathionylation and formation of a disulfide [1].

Chemical compound and disease context of GRX4

  • Remarkably, this disulfide of Grx4 was a direct substrate for NADPH and E. coli thioredoxin reductase, whereas the mixed disulfide was reduced by Grx1 [1].

Biological context of GRX4

  • However, our results also suggest that Grx3 and Grx4 might play additional roles in the oxidative stress response through proteins other than Aft1 [4].
  • The absence of both Grx3 and Grx4 induced a clear enrichment of G1 cells in asynchronous cultures, a slow growth phenotype, the accumulation of intracellular iron and a constitutive activation of the genes regulated by Aft1 [4].

Anatomical context of GRX4


Associations of GRX4 with chemical compounds

  • Grx4 is highly abundant (750-2000 ng/mg of total soluble protein), as determined by a specific enzyme-link immunosorbent assay, and most likely regulated by guanosine 3',5'-tetraphosphate upon entry to stationary phase [1].

Regulatory relationships of GRX4


Other interactions of GRX4

  • The mitochondrial forms of Grx3 and Grx4 partially rescue the defects of a grx5 null mutant [7].
  • Overexpression of Grx4 attenuates wild type Aft1 activity [3].


  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. 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]
  4. Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae. Pujol-Carrion, N., Belli, G., Herrero, E., Nogues, A., de la Torre-Ruiz, M.A. J. Cell. Sci. (2006) [Pubmed]
  5. 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]
  6. Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein. Bellí, G., Polaina, J., Tamarit, J., De La Torre, M.A., Rodríguez-Manzaneque, M.T., Ros, J., Herrero, E. J. Biol. Chem. (2002) [Pubmed]
  7. 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]
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