%0 Journal Article
%T Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2
%A Aleksandra Lewandowska
%A David Young
%A Didier Vertommen
%A Frank Van Breusegem
%A Joris Messens
%A Khadija Wahni
%A Thuy-Dung Ho Nguyen
%A Trung Nghia Vo
%J Antioxidants | An Open Access Journal from MDPI
%D 2019
%R https://doi.org/10.3390/antiox8010008
%X Members of the DJ-1 protein family are multifunctional enzymes whose loss increases the susceptibility of the cell to oxidative stress. However, little is known about the function of the plant DJ-1 homologs. Therefore, we analyzed the effect of oxidation on the structure and function of chloroplastic AtDJ-1B and studied the phenotype of T-DNA lines lacking the protein. In vitro oxidation of AtDJ-1B with H 2O 2 lowers its glyoxalase activity, but has no effect on its holdase chaperone function. Remarkably, upon oxidation, the thermostability of AtDJ-1B increases with no significant alteration of the overall secondary structure. Moreover, we found that AtDJ-1B transcript levels are invariable, and loss of AtDJ-1B does not affect plant viability, growth and stress response. All in all, two discrete functions of AtDJ-1B respond differently to H 2O 2, and AtDJ-1B is not essential for plant development under stress. View Full-Tex
%U https://www.mdpi.com/2076-3921/8/1/8