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In vivo detection of protein cysteine sulfenylation in plastids
Journal Contribution - Journal Article
Protein cysteine thiols are postU+2010translationally modified under oxidative stress conditions. Illuminated chloroplasts are one of the important sources of hydrogen peroxide (H2O2) and are highly sensitive to environmental stimuli, yet a comprehensive view of the oxidationU+2010sensitive chloroplast proteome is still missing. By targeting the sulfenic acid YAP1CU+2010trapping technology to the plastids of lightU+2010grown Arabidopsis cells, we identified 132 putatively sulfenylated plastid proteins upon H2O2 pulse treatment. Almost half of the sulfenylated proteins are enzymes of the amino acid metabolism. Using metabolomics, we observed a reversible decrease in the levels of the amino acids Ala, Asn, Cys, Gln, Glu, His, Ile, Leu, Lys, Phe, Ser, Thr and Val after H2O2 treatment, which is in line with an anticipated decrease in the levels of the glycolysis and tricarboxylic acid metabolites. Through the identification of an organelleU+2010tailored proteome, we demonstrated that the subcellular targeting of the YAP1C probe enables us to study in vivo cysteine sulfenylation at the organellar level. All in all, the identification of these oxidation events in plastids revealed that several enzymes of the amino acid metabolism rapidly undergo cysteine oxidation upon oxidative stress.
Journal: Plant Journal
Pages: 765 - 778