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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).
Author
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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
chaperone, glyoxalase, holdase, redox, PROTEIN SECONDARY STRUCTURE, MOLECULAR CHAPERONE, ESCHERICHIA-COLI, METHYLGLYOXAL, STRESS, SUPERFAMILY, HSP31, GLYCATION, MEMBER, PHOTOSYNTHESIS

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MLA
Lewandowska, Aleksandra 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.
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).
Chicago author-date
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).
Chicago author-date (all authors)
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).
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. 2019;8(1).
IEEE
[1]
A. Lewandowska et al., “Bifunctional chloroplastic DJ-1B from Arabidopsis thaliana is an oxidation-robust holdase and a glyoxalase sensitive to H2O2,” ANTIOXIDANTS, vol. 8, no. 1, 2019.
@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},
  keywords     = {chaperone,glyoxalase,holdase,redox,PROTEIN SECONDARY STRUCTURE,MOLECULAR CHAPERONE,ESCHERICHIA-COLI,METHYLGLYOXAL,STRESS,SUPERFAMILY,HSP31,GLYCATION,MEMBER,PHOTOSYNTHESIS},
  language     = {eng},
  number       = {1},
  pages        = {18},
  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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