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Sulfenome mining in Arabidopsis thaliana

  • Waszczak, Cezary
  • Akter, Mosammat 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
Publication Date
Jan 01, 2014
Ghent University Institutional Archive
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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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