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 |
Journal | Antioxidants (Basel) |
Volume | 8 |
Issue | 1 |
Date Published | 2019 Jan 01 |
ISSN | 2076-3921 |
Abstract | 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. |
DOI | 10.3390/antiox8010008 |
Alternate Journal | Antioxidants (Basel) |
PubMed ID | 30609642 |
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 / |
- Log in to post comments
- Google Scholar
- PubMed
- DOI