Identification of A. thaliana 2-Cys peroxiredoxins interacting proteins

Peroxiredoxins are ubiquitous thiol-dependent peroxidases for which chaperone and signaling roles have been reported in various types of organisms in the last years. In plants, the peroxidase function of the two typical plastidial 2-Cys peroxiredoxins (2-Cys PRX A and B) has been highlighted while the other functions, particularly in ROS-dependent signal transduction pathways, are still elusive due notably to the lack of knowledge on interacting partners. Using an ex vivo approach based on co-immunoprecipitation of leaf extracts from Arabidopsis thaliana wild-type and mutant plants lacking 2-Cys PRX expression followed by mass spectrometry-based proteomics, 158 proteins were found associated to 2-Cys PRXs, notably already known partners like thioredoxin-related electron donors (Chloroplastic Drought-induced Stress Protein of 32 kDa, Atypical Cysteine Histidine rich Thioredoxin 2) and enzymes involved in chlorophyll synthesis (Protochlorophyllide OxidoReductase B) or carbon metabolisms (Fructose-1,6-BisPhosphatase), validating the relevance of this approach.