Thiol-disulphide independent in-cell trapping for the identification of peroxiredoxin 2 interactors.

ABSTRACT: Hydrogen peroxide (H₂O₂) acts as a signalling molecule by oxidising cysteine thiols in proteins. Recent evidence has established a role for cytosolic peroxiredoxins in transmitting H₂O₂-based oxidation to a multitude of target proteins. Moreover, it is becoming clear that peroxiredoxins fulfil their function in organised microdomains, where not all interactors are covalently bound. However, most studies aimed at identifying peroxiredoxin interactors were based on methods that only detect covalently linked partners. Here, we explore the applicability of two thiol-disulphide independent in-cell trapping methodological approaches in combination with mass spectrometry for the identification of interaction partners of peroxiredoxin 2 (Prdx2). The firs

SUBMITTER: Luo T 

PROVIDER: S-EPMC8346688 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature