Sulfenome mining in Arabidopsis thaliana.

TitleSulfenome mining in Arabidopsis thaliana.
Publication TypeJournal Article
Year of Publication2014
AuthorsWaszczak, 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.
JournalProc Natl Acad Sci U S A
Volume111
Issue31
Pagination11545-50
Date Published2014 Aug 05
ISSN1091-6490
KeywordsArabidopsis, 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
Abstract

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.

DOI10.1073/pnas.1411607111
Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID25049418
PubMed Central IDPMC4128149
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