Sulfenome mining in Arabidopsis thaliana
2014
Waszczak, Cezary | Akter, Salma | Eeckhout, Dominique | Persiau, Geert | Wahni, Khadija | Bodra, Nandita | Van Molle, Inge | De Smet, Barbara | Vertommen, Didier | Gevaert, Kris | De Jaeger, Geert | Van Montagu, Marc | Messens, Joris | Van Breusegem, Frank
Reactive oxygen species (ROS) have been shown to be potent signaling molecules. Today, oxidation of cysteine residues is a well-recognized posttranslational protein modification, but the signaling processes steered by such oxidations are poorly understood. To gain insight into the cysteine thiol-dependent ROS signaling in Arabidopsis thaliana , we identified the hydrogen peroxide (H ₂O ₂)-dependent sulfenome: that is, proteins with at least one cysteine thiol oxidized to a sulfenic acid. By means of a genetic construct consisting of a fusion between the C-terminal domain of the yeast (Saccharomyces cerevisiae) AP-1–like (YAP1) transcription factor and a tandem affinity purification tag, we detected ∼100 sulfenylated proteins in Arabidopsis cell suspensions exposed to H ₂O ₂ stress. The in vivo YAP1-based trapping of sulfenylated proteins was validated by a targeted in vitro analysis of DEHYDROASCORBATE REDUCTASE2 (DHAR2). In DHAR2, the active site nucleophilic cysteine is regulated through a sulfenic acid-dependent switch, leading to S-glutathionylation, a protein modification that protects the protein against oxidative damage.
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