Description
Hydrogen peroxide (H2O2) is an important messenger molecule for diverse cellular processes. H2O2 oxidizes cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, and this reaction affects protein functions. Although many proteins have been identified as potential targets of S-sulfenylation in plants, site-specific mapping and quantification of S-sulfenylation remained largely unknown. Using peptide-centric chemoproteomics, we mapped 1,537 S-sulfenylated sites on more than 1,000 proteins in Arabidopsis cells. We quantified the redox-sensitivity of more than 70% of these endogenous oxidation events towards exogenous H2O2 stimulation. Proteins from translation and carbon metabolism are identified as hotspots for S-sulfenylation and hint towards redox regulation of these processes. S-sulfenylation is also observed in several catalytic sites, and metal-binding sites. By comparing human and Arabidopsis S-sulfenylated protein sites, we identified 124 conserved redox-sensitive cysteines. To show the impact on protein functionality, we report on the redox sensitivity of a non-catalytic conserved cysteine in a mitogen-activated protein kinase. In summary, we quantitatively mapped the redox sensitive cysteines of Arabidopsis under oxidative stress, and deliver an unprecedented basis for understanding their role in redox signaling in plants.| Period | 29 Apr 2019 → 3 May 2019 |
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| Event title | VII Brazilian Symposium on Plant Molecular Genetics |
| Event type | Conference |
| Location | Sao Paulo, BrazilShow on map |
| Degree of Recognition | International |