Disease relevance of GRX3

• Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3), all containing the classic dithiol active site CPYC [1].

High impact information on GRX3

• Grx3 and Grx4 interact with Aft1 as shown by two-hybrid interactions and co-immunoprecipitation assays [2].
• Here we have shown that Grx3 locates at the nucleus and that the thioredoxin-like domain is required for such location [3].
• Grx5 defines a family of yeast monothiol glutaredoxins that also includes Grx3 and Grx4 [4].
• Here we demonstrate that Grx3, Grx4 and Aft1 interact each other both in vivo and in vitro, which suggests the existence of a functional protein complex [5].
• Fluorescence microscopy revealed that Grx3 is targeted to nuclear rim and endoplasmic reticulum, Grx4 primarily to the nucleus, and Grx5 to mitochondria [6].

Biological context of GRX3

• However, our results also suggest that Grx3 and Grx4 might play additional roles in the oxidative stress response through proteins other than Aft1 [5].
• 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 [5].

Anatomical context of GRX3

• Grx5 is involved in iron/sulfur cluster assembly at the mitochondria, but the function of Grx3 and Grx4 is unknown [4].

Associations of GRX3 with chemical compounds

• The fission yeast Schizosaccharomyces pombe contains two dithiol glutaredoxins (Grx1 and Grx2) and genes for three putative monothiol glutaredoxins (grx3, 4, and 5) [6].

Other interactions of GRX3

• Null mutation of grx3 did not significantly affect growth and resistance against various oxidants, whereas grx5 mutation caused slow growth and sensitivity toward oxidants such as hydrogen peroxide, paraquat, and diamide [6].
• Thus, Grx3 and Grx4 are novel components required for Aft1 iron regulation that most likely occurs in the nucleus [2].

References