|Title||Bifunctional Chloroplastic DJ-1B from is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H₂O₂.|
|Publication Type||Journal Article|
|Year of Publication||2019|
|Authors||Lewandowska, A., T. Nghia Vo, T-D. Ho Nguyen, K. Wahni, D. Vertommen, F. Van Breusegem, D. Young, and J. Messens|
|Date Published||2019 Jan 01|
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 H₂O₂ 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 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 H₂O₂, and AtDJ-1B is not essential for plant development under stress.
|Alternate Journal||Antioxidants (Basel)|
|PubMed Central ID||PMC6356872|
|Grant List||30829584 / / Research Foundation-Flanders Excellence of Science project / |
G0D7914N / / Research Foundation-Flanders /
SRP34 / / Strategic Research Programme VUB /
HERC16 / / Hercules foundation /
to A.L. / / VIB International PhD program /
Bifunctional Chloroplastic DJ-1B from is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H₂O₂.