Differential inhibition of Arabidopsis superoxide dismutases by peroxynitrite-mediated tyrosine nitration

Holzmeister, Christian; Gaupels, Frank; Geerlof, Arie; Sarioglu, Hakan; Sattler, Michael; Durner, Jörg; Lindermayr, Christian

doi:10.1093/jxb/eru458

Cited by 106 publications

(63 citation statements)

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“…Thus, this enzyme is an important regulator of cellular redox homeostasis and signaling. Interestingly, Arabidopsis superoxide dismutases are differentially inhibited by peroxinitrite, suggesting a regulatory function under stress conditions (Holzmeister et al, 2015).All these studies demonstrate the importance of the interplay between $NO and ROS. They illustrate that $NO and ROS signaling can underlay synergistic or antagonistic mechanisms or function in parallel.…”

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confidence: 73%

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Interplay of Reactive Oxygen Species and Nitric Oxide: Nitric Oxide Coordinates Reactive Oxygen Species Homeostasis

Lindermayr

Durner

2015

Plant Physiol.

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Redox reactions are evolutionarily a very old signaling principle, which occur in prokaryotes and eukaryotes. The most important redox molecules are reactive oxygen species (ROS), such as singlet oxygen, hydroxyl radical, superoxide anion, hydrogen peroxide, and nitric oxide ($NO). In plants, they have very important signaling functions and are involved in the regulation of transpiration, gas exchange, plant defense response, cell death, germination, and plant growth and development. The diverse functions may be explained by the fact that ROS and $NO interact rapidly to form a number of reactive nitrogen species, such as ONOO 2 , NO 2 , N 2 O 3 , and other NO x species. Besides the direct interactions of these redox molecules, both molecules can act as oxidizing agents on proteins, and in this way they can modify the activity or function of proteins involved in $NO and ROS signaling as well as metabolism and homeostasis.The first evidence for a physiological interplay between $NO and ROS was provided by Delledonne et al. (2001). They demonstrated that hypersensitive cell death is only triggered by balanced production of $NO and ROS and that interaction of $NO with hydrogen peroxide is required. Additionally, as part of the innate immune response in Arabidopsis (Arabidopsis thaliana), $NO inhibits NADPH oxidase and regulates cell death (Yun et al., 2011). Moreover, in guard cells, $NO and ROS act in concert with abscisic acid during stomatal closure (Bright et al., 2006).Physiologically, ROS and $NO have both beneficial and deleterious effects, depending upon the concentration and exposure time. Plants have developed effective mechanisms to control ROS levels, protecting themselves from oxidative damage on one side, and they also use ROS as signaling molecules on the other side. ROS are detoxified by the glutathione-ascorbate cycle. The cycle involves the antioxidant metabolites: ascorbate, glutathione, and NADPH and the enzymes linking these metabolites, among them ascorbate oxidase (Noctor and Foyer, 1998). In this issue, Yang et al. (2015) add a new and important aspect to the interplay of $NO and ROS metabolism and control: the regulation of the ROSdegrading enzyme ascorbate peroxidase by nitric oxide. They demonstrated that $NO positively regulates the activity of cytosolic ASCORBATE PEROXIDASE1 by S-nitrosylation of Cys-32. S-Nitrosylation of this residue results in an enhanced resistance to oxidative stress and positively affects the immune response. Interestingly, pea (Pisum sativum) cytosolic ASCORBATE PEROXI-DASE1 is regulated by $NO in a dual way. While S-nitrosylation enhances its activity, Tyr nitration results in inhibition (Begara-Morales et al., 2014), demonstrating the complexity of the $NO and ROS interplay.A connection between $NO and ROS has also been demonstrated for other antioxidant enzymes, such as peroxiredoxin II E and superoxide dismutase. S-Nitrosylation of Arabidopsis peroxiredoxin II E inhibits its hydrogen peroxide-reducing and peroxinitrite-detoxifying activities, and in this way, ...

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confidence: 73%

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confidence: 99%

Interplay of Reactive Oxygen Species and Nitric Oxide: Nitric Oxide Coordinates Reactive Oxygen Species Homeostasis

Lindermayr

Durner

2015

Plant Physiol.

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“…Nitration, on the other hand, can be defined as the addition of a nitro-group (−NO 2 ) to protein aromatic amino acids such as tyrosine or tryptophan [57,58]. The in vivo mechanism of protein nitration is mediated by the intermediate formation of tyrosine or tryptophan free radicals and subsequent reactions with either • NO or • NO 2 1 .…”

Section: Homeostatic Regulation Of Nitrosylationmentioning

confidence: 99%

“…The in vivo mechanism of protein nitration is mediated by the intermediate formation of tyrosine or tryptophan free radicals and subsequent reactions with either • NO or • NO 2 1 . It should also be emphasized that to date there is no evidence of a direct bimolecular reaction of tryptophan or tyrosine with peroxynitrite [58,59]. This area can be somewhat confusing, and hence, we have included Fig.…”

Section: Homeostatic Regulation Of Nitrosylationmentioning

confidence: 99%

Nitrosative Stress, Hypernitrosylation, and Autoimmune Responses to Nitrosylated Proteins: New Pathways in Neuroprogressive Disorders Including Depression and Chronic Fatigue Syndrome

Morris¹,

Berk

Klein

et al. 2016

Mol Neurobiol

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Nitric oxide plays an indispensable role in modulating cellular signaling and redox pathways. This role is mainly effected by the readily reversible nitrosylation of selective protein cysteine thiols. The reversibility and sophistication of this signaling system is enabled and regulated by a number of enzymes which form part of the thioredoxin, glutathione, and pyridoxine antioxidant systems. Increases in nitric oxide levels initially lead to a defensive increase in the number of nitrosylated proteins in an effort to preserve their function. However, in an environment of chronic oxidative and nitrosative stress (O&NS), nitrosylation of crucial cysteine groups within key enzymes of the thioredoxin, glutathione, and pyridoxine systems leads to their inactivation thereby disabling denitrosylation and transnitrosylation and subsequently a state described as "hypernitrosylation." This state leads to the development of pathology in multiple domains such as the inhibition of enzymes of the electron transport chain, decreased mitochondrial function, and altered conformation of proteins and amino acids leading to loss of immune tolerance and development of autoimmunity. Hypernitrosylation also leads to altered function or inactivation of proteins involved in the regulation of apoptosis, autophagy, proteomic degradation, transcription factor activity, immune-inflammatory pathways, energy production, and neural function and survival. Hypernitrosylation, as a consequence of chronically elevated O&NS and activated immune-inflammatory pathways, can explain many characteristic abnormalities observed in neuroprogressive disease including major depression and chronic fatigue syndrome/myalgic encephalomyelitis. In those disorders, increased bacterial translocation may drive hypernitrosylation and autoimmune responses against nitrosylated proteins.

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“…45 Differential inhibition of mitochondrial MnSOD, peroxisomal Cu/ZnSOD and chloroplastic FeSOD has also been reported in Arabidposis thaliana due to peroxinitrite-mediated tyrosine nitration (Tyr63). 46 To sum up, total SOD activity in sunflower cotyledons or roots is modulated owing to differential response of the 2 isoforms (FeSOD and Cu/ZnSOD) to NaCl stress. The observed differential spatial distribution of the 2 isoforms (MnSOD and Cu/ZnSOD) in seedling cotyledons and their sensitivity to salt stress in 2d old seedlings indicates their crucial role in subcellular management of superoxide anion production as a rapid stress response.…”

Section: E1071753-6mentioning

confidence: 99%

Nitric oxide triggers a concentration-dependent differential modulation of superoxide dismutase (FeSOD and Cu/ZnSOD) activity in sunflower seedling roots and cotyledons as an early and long distance signaling response to NaCl stress

Arora

Bhatla

2015

Plant Signaling & Behavior

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Differential inhibition of Arabidopsis superoxide dismutases by peroxynitrite-mediated tyrosine nitration

Abstract: SummarySuperoxide dismutases (SODs) are differentially inhibited by peroxynitrite-mediated tyrosine nitration. Tyr63 is the main target responsible for inactivation of MnSOD1. This mechanism seems to be evolutionarily conserved in multicellular organisms.

Cited by 106 publications

References 43 publications

Interplay of Reactive Oxygen Species and Nitric Oxide: Nitric Oxide Coordinates Reactive Oxygen Species Homeostasis

Interplay of Reactive Oxygen Species and Nitric Oxide: Nitric Oxide Coordinates Reactive Oxygen Species Homeostasis

Nitrosative Stress, Hypernitrosylation, and Autoimmune Responses to Nitrosylated Proteins: New Pathways in Neuroprogressive Disorders Including Depression and Chronic Fatigue Syndrome

Nitric oxide triggers a concentration-dependent differential modulation of superoxide dismutase (FeSOD and Cu/ZnSOD) activity in sunflower seedling roots and cotyledons as an early and long distance signaling response to NaCl stress

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