title: Sulfenome mining in Arabidopsis thaliana.
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.
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;Structural Biology Research Center, VIB, 1050 Brussels, Belgium;Brussels Center for Redox Biology, 1050 Brussels, Belgium;Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
authors: Cezary
authors: C
authors: Waszczak
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;Structural Biology Research Center, VIB, 1050 Brussels, Belgium;Brussels Center for Redox Biology, 1050 Brussels, Belgium;Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium;Department of Fisheries, Faculty of Biological Sciences, University of Dhaka, 1000 Dhaka, Bangladesh;
authors: Salma
authors: S
authors: Akter
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;
authors: Dominique
authors: D
authors: Eeckhout
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;
authors: Geert
authors: G
authors: Persiau
authors: Structural Biology Research Center, VIB, 1050 Brussels, Belgium;Brussels Center for Redox Biology, 1050 Brussels, Belgium;Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
authors: Khadija
authors: K
authors: Wahni
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;Structural Biology Research Center, VIB, 1050 Brussels, Belgium;Brussels Center for Redox Biology, 1050 Brussels, Belgium;Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
authors: Nandita
authors: N
authors: Bodra
authors: Structural Biology Research Center, VIB, 1050 Brussels, Belgium;Brussels Center for Redox Biology, 1050 Brussels, Belgium;Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
authors: Inge
authors: I
authors: Van Molle
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;Structural Biology Research Center, VIB, 1050 Brussels, Belgium;Brussels Center for Redox Biology, 1050 Brussels, Belgium;Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium;
authors: Barbara
authors: B
authors: De Smet
authors: de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium;
authors: Didier
authors: D
authors: Vertommen
authors: Department of Medical Protein Research, VIB, 9000 Ghent, Belgium; andDepartment of Biochemistry, Ghent University, 9000 Gent, Belgium.
authors: Kris
authors: K
authors: Gevaert
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium;
authors: Geert
authors: G
authors: De Jaeger
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be joris.messens@vib-vub.be frank.vanbreusegem@psb.vib-ugent.be.
authors: Marc
authors: M
authors: Van Montagu
authors: Structural Biology Research Center, VIB, 1050 Brussels, Belgium;Brussels Center for Redox Biology, 1050 Brussels, Belgium;Structural Biology Brussels Laboratory, Vrije Universiteit Brussel, 1050 Brussels, Belgium; marc.vanmontagu@ugent.be joris.messens@vib-vub.be frank.vanbreusegem@psb.vib-ugent.be.
authors: Joris
authors: J
authors: Messens
authors: Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium;Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; marc.vanmontagu@ugent.be joris.messens@vib-vub.be frank.vanbreusegem@psb.vib-ugent.be.
authors: Frank
authors: F
authors: Van Breusegem
mesh_terms: D017360:Arabidopsis / Q000187:drug effects / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007700:Kinetics; D055442:Metabolome / Q000187:drug effects; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000378:metabolism; D010084:Oxidation-Reduction / Q000187:drug effects; D018384:Oxidative Stress / Q000187:drug effects; D011485:Protein Binding / Q000187:drug effects; D059748:Proteolysis / Q000187:drug effects; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000187:drug effects; D013434:Sulfenic Acids / Q000378:metabolism*; D013997:Time Factors
chemical_list: D029681:Arabidopsis Proteins; D046912:Multiprotein Complexes; D011993:Recombinant Fusion Proteins; D013434:Sulfenic Acids; D006861:Hydrogen Peroxide; D005978:Glutathione; D003545:Cysteine
keywords: cysteine oxidation; oxidative stress; redox regulation