|Title||Sulfenome mining in Arabidopsis thaliana.|
|Publication Type||Journal Article|
|Year of Publication||2014|
|Authors||Waszczak, C., S. Akter, D. Eeckhout, G. Persiau, K. Wahni, N. Bodra, I. Van Molle, B. De Smet, D. Vertommen, K. Gevaert, G. De Jaeger, M. Van Montagu, J. Messens, and F. Van Breusegem|
|Journal||Proc Natl Acad Sci U S A|
|Date Published||2014 Aug 05|
|Keywords||Arabidopsis, Arabidopsis Proteins, Cysteine, Glutathione, Hydrogen Peroxide, Kinetics, Metabolome, Models, Biological, Multiprotein Complexes, Oxidation-Reduction, Oxidative Stress, Protein Binding, Proteolysis, Recombinant Fusion Proteins, Signal Transduction, Sulfenic Acids, Time Factors|
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 (H2O2)-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 H2O2 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.
|Alternate Journal||Proc. Natl. Acad. Sci. U.S.A.|
|PubMed Central ID||PMC4128149|
Sulfenome mining in Arabidopsis thaliana.