期刊
MOLECULAR & CELLULAR PROTEOMICS
卷 14, 期 5, 页码 1183-1200出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M114.046896
关键词
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资金
- VUB grant [HOA 22]
- Research Foundation Flanders (FWO) [G0D7914N]
- NIH [GM102187, CA174986]
- IWT
- Erasmus Mundus External Cooperation Window
- Ghent University [01MRB510W]
- Interuniversity Attraction Poles Program [IUAP P7/29 MARS]
- Belgian Science Police Office
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.
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