Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress.

TitleProtein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress.
Publication TypeJournal Article
Year of Publication2015
AuthorsJacques, S., Ghesquière B., De Bock P-J., Demol H., Wahni K., Willems P., Messens J., Van Breusegem F., and Gevaert K.
JournalMol Cell Proteomics
Volume14
Issue5
Pagination1217-29
Date Published2015 May
ISSN1535-9484
KeywordsArabidopsis, Arabidopsis Proteins, Gene Deletion, Glutathione Transferase, Hydrogen Peroxide, Isoenzymes, Kinetics, Methionine, Molecular Sequence Annotation, Oxidation-Reduction, Oxidative Stress, Plant Leaves, Plants, Genetically Modified, Protein Processing, Post-Translational
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.

DOI10.1074/mcp.M114.043729
Alternate JournalMol. Cell Proteomics
PubMed ID25693801
PubMed Central IDPMC4424394
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