A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation.

ABSTRACT: Hydrogen peroxide (H₂O₂) acts as a signaling messenger by triggering the reversible oxidation of redox-regulated proteins. It remains unclear how proteins can be oxidized by signaling levels of H₂O₂ in the presence of peroxiredoxins, which are highly efficient peroxide scavengers. Here we show that the rapid formation of disulfide bonds in cytosolic proteins is enabled, rather than competed, by cytosolic 2-Cys peroxiredoxins. Under the conditions tested, the combined deletion or depletion of cytosolic peroxiredoxins broadly frustrated H₂O₂-dependent protein thiol oxidation, which is the exact opposite of what would be predicted based on the assumption that H₂O₂ oxidizes proteins directly. We find that p

SUBMITTER: Stocker S 

PROVIDER: S-EPMC5863949 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature