< Terug naar vorige pagina

Publicatie

Sulfenome mining in Arabidopsis thaliana

Tijdschriftbijdrage - Tijdschriftartikel

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.
Tijdschrift: Proc Natl Acad Sci USA
ISSN: 0027-8424
Volume: 111
Pagina's: 11545-11550
Jaar van publicatie:2014
Trefwoorden:cysteine oxidation, oxidative stress, redox regulation
  • ORCID: /0000-0003-0114-9379/work/105289548
  • Scopus Id: 84905667050