期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 31, 页码 11545-11550出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1411607111
关键词
oxidative stress; redox regulation; cysteine oxidation
资金
- Ghent University Multidisciplinary Research Partnership [01MRB 510W]
- Bijzondere Onderzoeksfonds [BOF 01J11311]
- Interuniversity Attraction Poles Program [IUAP VII/29]
- Belgian State, Science Policy Office
- Research Foundation-Flanders [G.0D.79.14N, G.0038.09N]
- European Cooperation in Science and Research (COST Action) [BM1203/EU-ROS]
- VIB International PhD Program predoctoral fellowship
- Erasmus Mundus External Cooperation Window predoctoral fellowship
- Omics@vib Marie Curie COFUND fellowship
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 similar to 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.
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