Protein carbonylation is a non-enzymatic and irreversible post-translational modification that occurs naturally in living organisms under the direct or indirect effect of reactive oxygen species (ROS). In this study, we analyzed proteins that are responsive to carbonylation by exogenous hydrogen peroxide (H2O2) by profiling the carbonylated proteome extracted from Arabidopsis thaliana leaves after H2O2 treatment. Carbonylated proteins were enriched at the peptide level and analyzed by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS). The results revealed that most of the carbonylated proteins identified in the H2O2-treated plant samples are related to sulphate adenylyl transferases and amidophosphoribosyl transferases involved in the immune system response, defense response, and external stimulus-response.
[doi:10.25345/C57H1DR8X]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Cyanine hydrazide ; Hydrogen peroxide ; Metal-catalyzed oxidation ; Plant defense response ; carbonylated proteins ; Reactive electrophile species
Principal Investigators: (in alphabetical order) |
Tagnon Missihoun, University of Quebec Trois-Rivieres, Canada |
Submitting User: | Tagnon |
Fangue-Yapseu GY, Tola AJ, Missihoun TD.
Proteome-wide analysis of hydrogen peroxide-induced protein carbonylation in Arabidopsis thaliana.
Front Plant Sci. Epub 2022 Dec 5.
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