Prdx1 Interacts with ASK1 upon Exposure to HO and Independently of a Scaffolding Protein.

Hydrogen peroxide (HO) is a key redox signaling molecule that selectively oxidizes cysteines on proteins. It can accomplish this even in the presence of highly efficient and abundant HO scavengers, peroxiredoxins (Prdxs), as it is the Prdxs themselves that transfer oxidative equivalents to specific protein thiols on target proteins via their redox-relay functionality. The first evidence of a mammalian cytosolic Prdx-mediated redox-relay-Prdx1 with the kinase ASK1-was presented a decade ago based on the outcome of a co-immunoprecipitation experiment.

Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.

Peroxiredoxins (Prdxs) sense and assess peroxide levels, and signal through protein interactions. Understanding the role of the multiple structural and post-translational modification (PTM) layers that tunes the peroxiredoxin specificities is still a challenge. In this review, we give a tabulated overview on what is known about human and bacterial peroxiredoxins with a focus on structure, PTMs, and protein-protein interactions.

Bifunctional Chloroplastic DJ-1B from is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H₂O₂.

Members of the DJ-1 protein family are multifunctional enzymes whose loss increases the susceptibility of the cell to oxidative stress. However, little is known about the function of the plant DJ-1 homologs. Therefore, we analyzed the effect of oxidation on the structure and function of chloroplastic AtDJ-1B and studied the phenotype of T-DNA lines lacking the protein.