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Sulfenome mining in Arabidopsis thaliana

Authors
  • 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
Source
Ghent University Institutional Archive
Keywords
Language
English
License
Unknown
External links

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 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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