|Title||Identification of dimedone-trapped sulfenylated proteins in plants under stress.|
|Publication Type||Journal Article|
|Year of Publication||2017|
|Authors||Akter, S., S. Carpentier, F. Van Breusegem, and J. Messens|
|Journal||Biochem Biophys Rep|
|Date Published||2017 Mar|
In stressed plants, the reactive oxygen species (ROS) levels rise. Key to ROS signaling research are detection and identification of the protein cysteine sulfenylation (-SOH), the ROS-mediated oxidative product of a thiol (-SH). seedlings were stressed with hydrogen peroxide (HO) and the sulfenylated proteins were tagged with dimedone. Dimedone-tagged sulfenic acid proteins were visualized on a two-dimensional electrophoresis (2DE) immunoblot with an anticysteine sulfenic acid antibody and were subsequently detected by mass spectrometry. We optimized the detection method for protein sulfenylation in . We conclude that dimedone can penetrate the cell wall, does not stress plants, and can "read" the changes in the protein sulfenylation pattern under oxidative stress. We observed that the number of sulfenylated proteins in plants treated with 10 mM HO was higher than that in untreated plants. A total of 39 sulfenylated protein spots were found on 2DE immunoblots. By means of mass spectrometry, 11 sulfenylated proteins were discovered involved in primary metabolism, redox regulation, translation and signaling pathways. Hence, by combining an immunochemical 2DE strategy with mass spectrometry, we were able to identify sulfenylated proteins in HO-stressed seedlings. The sulfenylated proteins can be considered for further validation as redox regulators in plants.
|Alternate Journal||Biochem Biophys Rep|
|PubMed Central ID||PMC5632707|
Identification of dimedone-trapped sulfenylated proteins in plants under stress.