Identification of dimedone-trapped sulfenylated proteins in plants under stress.

TitleIdentification of dimedone-trapped sulfenylated proteins in plants under stress.
Publication TypeJournal Article
Year of Publication2017
AuthorsAkter, S., S. Carpentier, F. Van Breusegem, and J. Messens
JournalBiochem Biophys Rep
Volume9
Pagination106-113
Date Published2017 Mar
ISSN2405-5808
Abstract

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.

DOI10.1016/j.bbrep.2016.11.014
Alternate JournalBiochem Biophys Rep
PubMed ID29114583
PubMed Central IDPMC5632707
subject_category: 
Research group: