【摘 要】
：
Saccharomyces cerevisiae Grx3 and Grx4(Grx3/4)are two monothiol glutaredoxins that contain a thioredoxin(Trx)domain,followed by a glutaredoxin(Grx)domain.Grx3/4 not only play a key role in cellular de
【机 构】
：
School of Life Sciences,University of Science and Technology of China
【出 处】
：
中国生物化学与分子生物学会2016年全国学术会议
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Saccharomyces cerevisiae Grx3 and Grx4(Grx3/4)are two monothiol glutaredoxins that contain a thioredoxin(Trx)domain,followed by a glutaredoxin(Grx)domain.Grx3/4 not only play a key role in cellular defenses against oxidative stress,but also have been previously characterized as regulators of Aft1 localization and iron homeostasis.In iron sufficiency condition,Grx3/4,which originally form GSH-mediated iron-sulfur clustered homodimers,are proposed to form heterodimers with Fra2 to transmit this signal to Aft1 and Aft2.Interaction of Grx3/4 with Aft1 promotes dissociation of Aft1/2 from its target DNA,leading to down-regulation of Aft1/2 target genes.Here we solved the crystal structures of the individual Trx and Grx domains of Grx3.Cross-linking revealed that Trx-Grx interaction is mediated by a disulfide bond formed between Trx-Cys33 and Grx-Cys171.Enzymatic assays suggested that the Trx domain,especially the WAEPC motif contributes to the activity of the Grx domain.Furthermore,the NMR structure of Fra2 together with biochemical assays enable us to identify the interface of Fra2 and Grx3.But the binding affinity of Fra2-Grx3 is much lower than Fra2-Aft2.Taken together,these findings provide structural and catalytic insights into the multidomain thioredoxin-monothiol glutaredoxins,and also increase the understanding of the relationship between oxidative stress and iron homeostasis.
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