title: Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress.
abstract: Reactive oxygen species such as hydrogen peroxide can modify proteins via direct oxidation of their sulfur-containing amino acids, cysteine and methionine. Methionine oxidation, studied here, is a reversible posttranslational modification that is emerging as a mechanism by which proteins perceive oxidative stress and function in redox signaling. Identification of proteins with oxidized methionines is the first prerequisite toward understanding the functional effect of methionine oxidation on proteins and the biological processes in which they are involved. Here, we describe a proteome-wide study of in vivo protein-bound methionine oxidation in plants upon oxidative stress using Arabidopsis thaliana catalase 2 knock-out plants as a model system. We identified over 500 sites of oxidation in about 400 proteins and quantified the differences in oxidation between wild-type and catalase 2 knock-out plants. We show that the activity of two plant-specific glutathione S-transferases, GSTF9 and GSTT23, is significantly reduced upon oxidation. And, by sampling over time, we mapped the dynamics of methionine oxidation and gained new insights into this complex and dynamic landscape of a part of the plant proteome that is sculpted by oxidative stress.
authors.affiliation: From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium, Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium, Department of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Ghent, Belgium, Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 927, B-9052 Ghent, Belgium.
authors.forename: Silke
authors.initials: S
authors.lastname: Jacques
authors.affiliation: From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium, Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium.
authors.forename: Bart
authors.initials: B
authors.lastname: Ghesquière
authors.affiliation: From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium, Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium.
authors.forename: Pieter-Jan
authors.initials: PJ
authors.lastname: De Bock
authors.affiliation: From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium, Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium.
authors.forename: Hans
authors.initials: H
authors.lastname: Demol
authors.affiliation: VIB Structural Biology Research Center, Vrije Universiteit Brussel (VUB), B-1050 Brussels, Belgium, Brussels Center for Redox Biology, B-1050 Brussels, Belgium, Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.
authors.forename: Khadija
authors.initials: K
authors.lastname: Wahni
authors.affiliation: From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium, Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium, Department of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Ghent, Belgium, Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 927, B-9052 Ghent, Belgium.
authors.forename: Patrick
authors.initials: P
authors.lastname: Willems
authors.affiliation: VIB Structural Biology Research Center, Vrije Universiteit Brussel (VUB), B-1050 Brussels, Belgium, Brussels Center for Redox Biology, B-1050 Brussels, Belgium, Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.
authors.forename: Joris
authors.initials: J
authors.lastname: Messens
authors.affiliation: Department of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Ghent, Belgium, Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 927, B-9052 Ghent, Belgium, frank.vanbreusegem@psb.ugent.be.
authors.forename: Frank
authors.initials: F
authors.lastname: Van Breusegem
authors.affiliation: From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium, Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium, kris.gevaert@vib-ugent.be.
authors.forename: Kris
authors.initials: K
authors.lastname: Gevaert
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000032:analysis* / Q000235:genetics* / Q000378:metabolism; D017353:Gene Deletion; D005982:Glutathione Transferase / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism / Q000494:pharmacology; D007527:Isoenzymes / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008715:Methionine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D058977:Molecular Sequence Annotation; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D018515:Plant Leaves / Q000235:genetics / Q000378:metabolism; D030821:Plants, Genetically Modified; D011499:Protein Processing, Post-Translational
chemical_list: D029681:Arabidopsis Proteins; D007527:Isoenzymes; D008715:Methionine; D006861:Hydrogen Peroxide; C490276:CAT2 protein, Arabidopsis; C515223:GSTF9 protein, Arabidopsis; D005982:Glutathione Transferase; C013111:methionine sulfoxide