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Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2

(2019) Antioxidants. 8(1).
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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 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 H2O2, and AtDJ-1B is not essential for plant development under stress.
Keywords
Clinical Biochemistry, Cell Biology, Biochemistry, Physiology, Molecular Biology

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Chicago
Lewandowska, Aleksandra, Trung Vo, Thuy-Dung Nguyen, Khadija Wahni, Didier Vertommen, Frank Van Breusegem, David Young, and Joris Messens. 2019. “Bifunctional Chloroplastic DJ-1B from Arabidopsis Thaliana Is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2.” Antioxidants 8 (1).
APA
Lewandowska, A., Vo, T., Nguyen, T.-D., Wahni, K., Vertommen, D., Van Breusegem, F., Young, D., et al. (2019). Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2. Antioxidants, 8(1).
Vancouver
1.
Lewandowska A, Vo T, Nguyen T-D, Wahni K, Vertommen D, Van Breusegem F, et al. Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2. Antioxidants. MDPI AG; 2019;8(1).
MLA
Lewandowska, Aleksandra, Trung Vo, Thuy-Dung Nguyen, et al. “Bifunctional Chloroplastic DJ-1B from Arabidopsis Thaliana Is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2.” Antioxidants 8.1 (2019): n. pag. Print.
@article{8587414,
  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 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 H2O2, and AtDJ-1B is not essential for plant development under stress.},
  articleno    = {8},
  author       = {Lewandowska, Aleksandra and Vo, Trung and Nguyen, Thuy-Dung and Wahni, Khadija and Vertommen, Didier and Van Breusegem, Frank and Young, David and Messens, Joris},
  issn         = {2076-3921},
  journal      = {Antioxidants},
  keyword      = {Clinical Biochemistry,Cell Biology,Biochemistry,Physiology,Molecular Biology},
  language     = {eng},
  number       = {1},
  publisher    = {MDPI AG},
  title        = {Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2},
  url          = {http://dx.doi.org/10.3390/antiox8010008},
  volume       = {8},
  year         = {2019},
}

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