|Title||DYn-2 Based Identification of Arabidopsis Sulfenomes.|
|Publication Type||Journal Article|
|Year of Publication||2015|
|Authors||Akter, S., J. Huang, N. Bodra, B. De Smet, K. Wahni, D. Rombaut, J. Pauwels, K. Gevaert, K. Carroll, F. Van Breusegem, and J. Messens|
|Journal||Mol Cell Proteomics|
|Date Published||2015 May|
|Keywords||Arabidopsis, Arabidopsis Proteins, Avidin, Biotin, Cell Compartmentation, Cell Culture Techniques, Cyclohexanones, Hydrogen Peroxide, Molecular Probes, Molecular Sequence Annotation, Organelles, Oxidation-Reduction, Oxidative Stress, Protein Processing, Post-Translational, Proteomics, Signal Transduction, Sulfenic Acids|
Identifying the sulfenylation state of stressed cells is emerging as a strategic approach for the detection of key reactive oxygen species signaling proteins. Here, we optimized an in vivo trapping method for cysteine sulfenic acids in hydrogen peroxide (H2O2) stressed plant cells using a dimedone based DYn-2 probe. We demonstrated that DYn-2 specifically detects sulfenylation events in an H2O2 dose- and time-dependent way. With mass spectrometry, we identified 226 sulfenylated proteins after H2O2 treatment of Arabidopsis cells, residing in the cytoplasm (123); plastid (68); mitochondria (14); nucleus (10); endoplasmic reticulum, Golgi and plasma membrane (7) and peroxisomes (4). Of these, 123 sulfenylated proteins have never been reported before to undergo cysteine oxidative post-translational modifications in plants. All in all, with this DYn-2 approach, we have identified new sulfenylated proteins, and gave a first glance on the locations of the sulfenomes of Arabidopsis thaliana.
|Alternate Journal||Mol. Cell Proteomics|
|PubMed Central ID||PMC4424392|
|Grant List||R01 CA174864 / CA / NCI NIH HHS / United States |
R01 GM102187 / GM / NIGMS NIH HHS / United States
CA174986 / CA / NCI NIH HHS / United States
GM102187 / GM / NIGMS NIH HHS / United States
DYn-2 Based Identification of Arabidopsis Sulfenomes.