|Title||Sulfenome mining in Arabidopsis thaliana.|
|Publication Type||Journal Article|
|Year of Publication||2014|
|Authors||Waszczak, C., Akter S., Eeckhout D., Persiau G., Wahni K., Bodra N., Van Molle I., De Smet B., Vertommen D., Gevaert K., De Jaeger G., Van Montagu M., Messens J., and Van Breusegem F.|
|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.