Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage

Tossounian, Maria-Armineh; Molle, Inge Van; Wahni, Khadija; Jacques, Silke; Gevaert, Kris; Breusegem, Frank Van; Vertommen, Didier; Young, Diana; Rosado, Leonardo Astolfi; Messens, Joris

doi:10.1016/j.bbagen.2017.10.007

Cited by 20 publications

(25 citation statements)

References 65 publications

(69 reference statements)

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“…To test the ability of APxR to reduce H 2 O 2 , the FOX assay was performed as previously described [ 31 , 32 ]. Briefly, the reaction mixture contained APxR (0.5 µM or 5 µM) and 250 µM H 2 O 2 in 50 mM Tris/HCl pH 8, 0.3 M KCl.…”

Section: Methodsmentioning

confidence: 99%

Arabidopsis APx-R Is a Plastidial Ascorbate-Independent Peroxidase Regulated by Photomorphogenesis

et al. 2021

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Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide, thus minimizing cell injury and modulating signaling pathways as response to this reactive oxygen species. Using a phylogenetic approach, we previously identified a new peroxidase family composed of a small subset of ascorbate peroxidase (APx) homologs with distinguished features, which we named ascorbate peroxidase-related (APx-R). In this study, we showed that APx-R is an ascorbate-independent heme peroxidase. Despite being annotated as a cytosolic protein in public databases, transient expression of AtAPx-R-YFP in Arabidopsis thaliana protoplasts and stable overexpression in plants showed that the protein is targeted to plastids. To characterize APx-R participation in the antioxidant metabolism, we analyzed loss-of-function mutants and AtAPx-R overexpressing lines. Molecular analysis showed that glutathione peroxidase 7 (GPx07) is specifically induced to compensate the absence of APx-R. APx-R overexpressing lines display faster germination rates, further confirming the involvement of APx-R in seed germination. The constitutive overexpression of AtAPx-R-YFP unraveled the existence of a post-translational mechanism that eliminates APx-R from most tissues, in a process coordinated with photomorphogenesis. Our results show a direct role of APx-R during germinative and post-germinative development associated with etioplasts differentiation.

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Section: Methodsmentioning

confidence: 99%

Arabidopsis APx-R Is a Plastidial Ascorbate-Independent Peroxidase Regulated by Photomorphogenesis

et al. 2021

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“…Moreover, plants overexpressing MSRB7 display a higher abundance of GSTFs 2 and 3 in oxidative stress conditions, revealing preserved protein stability possibly through the maintenance of Met redox status. In full agreement, MetO formation due to H 2 O 2 treatment affects the activity of two other GSTs (GSTF9 and GSTT23) [ 110 ] and H 2 O 2 leads to preferential oxidation of Met14 in GSTT23, that could alter GSH binding and/or catalytic activity of the enzyme [ 127 ]. Moreover, Met oxidation in GSTF9 results in increased flexibility in the H-site responsible of substrate binding and in lower enzyme activity towards hydrophobic substrates [ 128 ].…”

Section: Mode Of Action and Substrates Of Plant Msrsmentioning

confidence: 97%

Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling

Rey

Tarrago

2018

Antioxidants

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Oxidation of methionine (Met) leads to the formation of two S- and R-diastereoisomers of Met sulfoxide (MetO) that are reduced back to Met by methionine sulfoxide reductases (MSRs), A and B, respectively. Here, we review the current knowledge about the physiological functions of plant MSRs in relation with subcellular and tissue distribution, expression patterns, mutant phenotypes, and possible targets. The data gained from modified lines of plant models and crop species indicate that MSRs play protective roles upon abiotic and biotic environmental constraints. They also participate in the control of the ageing process, as shown in seeds subjected to adverse conditions. Significant advances were achieved towards understanding how MSRs could fulfil these functions via the identification of partners among Met-rich or MetO-containing proteins, notably by using redox proteomic approaches. In addition to a global protective role against oxidative damage in proteins, plant MSRs could specifically preserve the activity of stress responsive effectors such as glutathione-S-transferases and chaperones. Moreover, several lines of evidence indicate that MSRs fulfil key signaling roles via interplays with Ca2+- and phosphorylation-dependent cascades, thus transmitting ROS-related information in transduction pathways.

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“…Also structural studies gave insight into the catalytic mechanisms and the role of MsrB as an antioxidant regulatory enzyme and methionine sulfoxide scavenger (19,20). In general, the catalytic mechanism of MsrB is similar to the one of MsrA.…”

Section: The Cys122-cys66 Disulfide For Trx Reduction and A Reversiblmentioning

confidence: 99%

Methionine sulfoxide reductase B from Corynebacterium diphtheriae catalyzes sulfoxide reduction via an intramolecular disulfide cascade

Tossounian

Truong

Buts

et al. 2020

Journal of Biological Chemistry

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Corynebacterium diphtheriae is a human pathogen that causes diphtheria. In response to immune system-induced oxidative stress, C. diphtheriae expresses antioxidant enzymes, among which are methionine sulfoxide reductase (Msr) enzymes, which are critical for bacterial survival in the face of oxidative stress. Although some aspects of the catalytic mechanism of the Msr enzymes have been reported, several details still await full elucidation. Here, we solved the solution structure of C. diphtheriae MsrB (Cd-MsrB) and unraveled its catalytic and oxidation-protection mechanisms. Cd-MsrB catalyzes methionine sulfoxide reduction involving three redox-active cysteines. Using NMR heteronuclear single-quantum coherence spectra, kinetics, biochemical assays, and MS analyses, we show that the conserved nucleophilic residue Cys-122 is S-sulfenylated after substrate reduction, which is then resolved by a conserved cysteine, Cys-66, or by the nonconserved residue Cys-127. We noted that the overall structural changes during the disulfide cascade expose the Cys-122–Cys-66 disulfide to recycling through thioredoxin. In the presence of hydrogen peroxide, Cd-MsrB formed reversible intra- and intermolecular disulfides without losing its Cys-coordinated Zn2+, and only the nonconserved Cys-127 reacted with the low-molecular-weight (LMW) thiol mycothiol, protecting it from overoxidation. In summary, our structure-function analyses reveal critical details of the Cd-MsrB catalytic mechanism, including a major structural rearrangement that primes the Cys-122–Cys-66 disulfide for thioredoxin reduction and a reversible protection against excessive oxidation of the catalytic cysteines in Cd-MsrB through intra- and intermolecular disulfide formation and S-mycothiolation.

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Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage

Cited by 20 publications

References 65 publications

Arabidopsis APx-R Is a Plastidial Ascorbate-Independent Peroxidase Regulated by Photomorphogenesis

Arabidopsis APx-R Is a Plastidial Ascorbate-Independent Peroxidase Regulated by Photomorphogenesis

Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling

Methionine sulfoxide reductase B from Corynebacterium diphtheriae catalyzes sulfoxide reduction via an intramolecular disulfide cascade

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