Comparison of structures among Saccharomyces cerevisiae Grxs proteins

Abstract

Glutaredoxins (Grxs) comprise a group of glutathione (GSH)-dependent oxidoreductase enzymes that respond to oxidative stress and sustain redox homeostasis. Saccharomyces cerevisiae Grx has a similar interaction patterns through its residues between the residues and the environment. The glutaredoxin domain covers 100% of the entire mature Grx1 and Grx8, while the glutaredoxin domain covers ~ 52% of the entire mature Grx6 and Grx7, which have approximately 74 additional amino acids in their N-terminal regions, whereas Grx3 and Grx4 have two functional domains: glutaredoxin and thioredoxin. We have presented the prediction of disordered regions within these protein sequences. Multiple sequence alignment combined with a phylogenetic tree enabled us to specify the key residues contributing to the differences between Saccharomyces cerevisiae Grxs and the proportion symmetry.

Metabolic Remodeling during Long-Lasting Cultivation of the Endomyces magnusii Yeast on Oxidative and Fermentative Substrates

“…The GPxs family contains eight selenium-dependent and non-selenium enzymes (GPx1-8), which catalyze the reduction of organic hydroperoxides and their alcohols via GSH [50]. A lack of GR leads to mortality in Sshizosaccaromyces pombe [51]. As GR/GP system activity is highly dependent on GSH concentrations, we speculate that the explanation for the stable GSH content of the yeast cells grown on both glycerol and glucose lies not only in the induction of GPxs but also in the regeneration of the GSH GR system, which maintains the redox balance in the cell.…”

Enhanced acetic acid stress tolerance and ethanol production in Saccharomyces cerevisiae by modulating expression of the de novo purine biosynthesis genes

“…However, no obvious difference of CAT enzyme among the engineered strains compared with that of the control, indicating that these genes endowed oxidation tolerance mainly through activation of SOD, which is consistent with the up-regulation of SOD1 . Meanwhile, an obvious increase of intracellular GSH, as well as elevated transcription of GSH1 , was observed in the three engineered strains, which contributed to protecting yeast cells against oxidative stress [37]. Higher GSH content was found also in the more tolerant yeast cells with zinc addition than that without zinc addition [12].…”

Effect of RNAi Targeting SeGrx1 on the Cytotoxicity and Insecticide Susceptibility of Camptothecin in Spodoptera exigua

“…They belong to the thioredoxin superfamily and have been proved to play essential functions in cellular redox homeostasis [2]. Until now, eight members of Grxs were found in Saccharomyces cerevisiae and five in Homo sapiens, and they are divided into three major categories based on the structure and catalytic properties [3,4]. The first group, referred to as class I, consists of Grx1 and Grx2, which are the typical Grxs with a characteristic Cys-X-X-Cys (CXXC) active site motif and a thioredoxin/glutaredoxin fold [3].…”

“…Until now, eight members of Grxs were found in Saccharomyces cerevisiae and five in Homo sapiens, and they are divided into three major categories based on the structure and catalytic properties [3,4]. The first group, referred to as class I, consists of Grx1 and Grx2, which are the typical Grxs with a characteristic Cys-X-X-Cys (CXXC) active site motif and a thioredoxin/glutaredoxin fold [3]. Grx1 exists widely in the mitochondrial inner membrane space, nucleus, and cytoplasm, and plays a role in oxidative stress and redox homeostasis [1,5].…”