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@article{3ae847ad60524efbabf6d69e459972e5,
title = "Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H₂O₂.",
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",
author = "Aleksandra Lewandowska and Trung Vo and Thuy-Dung Nguyen and Khadija Wahni and Didier Vertommen and Breusegem, {Frank Van} and David Young and Joris Messens",
year = "2019",
month = "1",
day = "1",
doi = "10.3390/antiox8010008",
language = "English",
volume = "8",
journal = "Antioxidants",
issn = "2076-3921",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "1",

}

RIS

TY - JOUR

T1 - Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H₂O₂.

AU - Lewandowska, Aleksandra

AU - Vo, Trung

AU - Nguyen, Thuy-Dung

AU - Wahni, Khadija

AU - Vertommen, Didier

AU - Breusegem, Frank Van

AU - Young, David

AU - Messens, Joris

PY - 2019/1/1

Y1 - 2019/1/1

N2 - 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.

AB - 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.

KW - Chaperone

KW - Glyoxalase

KW - Holdase

KW - Redox

UR - https://doi.org/10.3390/antiox8010008

UR - http://www.scopus.com/inward/record.url?scp=85060103209&partnerID=8YFLogxK

U2 - 10.3390/antiox8010008

DO - 10.3390/antiox8010008

M3 - Article

VL - 8

JO - Antioxidants

JF - Antioxidants

SN - 2076-3921

IS - 1

M1 - 8

ER -

ID: 44510708