A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses

Oberschall, Attila; Deák, Mária; Török, Katalin; Sass, László; Vass, Imre; Kovács, Izabella; Fehér, Attila; Dudits, Dénes; Horváth, Gábor

doi:10.1046/j.1365-313x.2000.00885.x

Cited by 216 publications

(113 citation statements)

References 34 publications

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“…Recently, an aldehyde reductase (37) has been identified in both the mitochondria and the cytoplasm that reacts with HNE. A glutathione S-transferase, which uses HNE as a substrate, has been identified in mammalian mitochondria (38,39) and in the monocot Sorghum bicolour (40).…”

Section: Discussionmentioning

confidence: 99%

Environmental Stress Causes Oxidative Damage to Plant Mitochondria Leading to Inhibition of Glycine Decarboxylase

Taylor¹,

Day²,

Millar³

2002

Journal of Biological Chemistry

175

145

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A cytotoxic product of lipid peroxidation, 4-hydroxy-2-nonenal (HNE), rapidly inhibited glycine, malate/ pyruvate, and 2-oxoglutarate-dependent O 2 consumption by pea leaf mitochondria. Dose-and timedependence of inhibition showed that glycine oxidation was the most severely affected with a K 0.5 of 30 M. Several mitochondrial proteins containing lipoic acid moieties differentially lost their reactivity to a lipoic acid antibody following HNE treatment. The most dramatic loss of antigenicity was seen with the 17-kDa glycine decarboxylase complex (GDC) H-protein, which was correlated with the loss of glycine-dependent O 2 consumption. Paraquat treatment of pea seedlings induced lipid peroxidation, which resulted in the rapid loss of glycine-dependent respiration and loss of Hprotein reactivity with lipoic acid antibodies. Pea plants exposed to chilling and water deficit responded similarly. In contrast, the damage to other lipoic acidcontaining mitochondrial enzymes was minor under these conditions. The implication of the acute sensitivity of glycine decarboxylase complex H-protein to lipid peroxidation products is discussed in the context of photorespiration and potential repair mechanisms in plant mitochondria.The polyunsaturated fatty acids of membrane lipids are susceptible to reactive oxygen species (ROS) 1 -induced peroxidation yielding various aldehydes, alkenals, and hydroxyalkenals, including the cytotoxic compounds malonaldehyde (MDA) and 4-hydroxy-2-nonenal (HNE). These two end products are commonly measured in studies of lipid peroxidation by the thiobarbituric acid-reactive substances (TBARS) assay (1). Interest in the biological effect of HNE was stimulated by studies showing cytotoxicity due to rapid reaction with sulfydryl groups via Michael addition (2). A number of stress conditions, including cardiac reperfusion injury, increase ROS production and the rate of membrane peroxidation and ultimately lead to inhibition of the respiratory rate in mammals (3). HNE has been shown to directly inhibit respiration of isolated mammalian mitochondria through modification of the lipoic acid moieties of 2-oxo acid dehydrogenases, forming HNE-Michael adducts ( Fig. 1) (4). These targets have also been shown to be damaged in vivo under conditions that induce lipid peroxidation (5).A range of biotic and abiotic stresses also raise ROS levels in plants due to perturbations of chloroplastic and mitochondrial metabolism and the generation of ROS in defense responses (6). Such accumulation of ROS in plants will clearly result in a wide variety of deleterious effects through oxidation reactions involving proteins, lipids, and nucleic acids. Lipid peroxidation in plants has been known for many years, but direct evidence of the pathways involved and the identification of HNE production in plants has only been reported recently (7). However, the exact molecular targets, the relative sensitivity of target enzymes, the mechanisms of repair, and the impact on plant function have not been extensively investigated.Research o...

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Section: Discussionmentioning

confidence: 99%

Environmental Stress Causes Oxidative Damage to Plant Mitochondria Leading to Inhibition of Glycine Decarboxylase

Taylor¹,

Day²,

Millar³

2002

Journal of Biological Chemistry

175

145

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“…Oberschall et al (27) have reported that overexpression of an alfalfa AKR contributed to improve plant tolerance to chemical and drought stresses through enhanced reduction of reactive aldehydes produced during lipid peroxidation. Interestingly, the alfalfa AKR is a homolog of AtChlAKR (At2g37770); the physiological significance of this class of AKR in plant species might therefore be the detoxification of reactive aldehydes.…”

Section: Aor Adr and Akr Cooperatively Scavenge Reactive Carbonyls mentioning

confidence: 99%

NADPH-dependent Reductases Involved in the Detoxification of Reactive Carbonyls in Plants

Yamauchi¹,

Hasegawa²,

Taninaka

et al. 2011

Journal of Biological Chemistry

151

117

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Reactive carbonyls, especially ␣,␤-unsaturated carbonyls produced through lipid peroxidation, damage biomolecules such as proteins and nucleotides; elimination of these carbonyls is therefore essential for maintaining cellular homeostasis. In this study, we focused on an NADPH-dependent detoxification of reactive carbonyls in plants and explored the enzyme system involved in this detoxification process. Using acrolein (CH 2 ‫؍‬ CHCHO) as a model ␣,␤-unsaturated carbonyl, we purified a predominant NADPH-dependent acrolein-reducing enzyme from cucumber leaves, and we identified the enzyme as an alkenal/one oxidoreductase (AOR) catalyzing reduction of an ␣,␤-unsaturated bond. Cloning of cDNA encoding AORs revealed that cucumber contains two distinct AORs, chloroplastic AOR and cytosolic AOR. Homologs of cucumber AORs were found among various plant species, including Arabidopsis, and we confirmed that a homolog of Arabidopsis (At1g23740) also had AOR activity. Phylogenetic analysis showed that these AORs belong to a novel class of AORs. They preferentially reduced ␣,␤-unsaturated ketones rather than ␣,␤-unsaturated aldehydes. Furthermore, we selected candidates of other classes of enzymes involved in NADPH-dependent reduction of carbonyls based on the bioinformatic information, and we found that an aldo-keto reductase (At2g37770) and aldehyde reductases (At1g54870 and At3g04000) were implicated in the reduction of an aldehyde group of saturated aldehydes and methylglyoxal as well as ␣,␤-unsaturated aldehydes in chloroplasts. These results suggest that different classes of NADPH-dependent reductases cooperatively contribute to the detoxification of reactive carbonyls.When plants are subjected to abiotic and/or biotic stresses, oxidative stress often results; this leads to the production of reactive oxygen species, which damage biomolecules such as proteins and lipids. More than half of the fatty acids found in the membranes of chloroplasts and mitochondria, two of the most highly oxidative organelles, are linoleic and linolenic acid. Because linoleic and linolenic acid are sources of many short chain carbonyls through their peroxidation (1), biomolecules in both types of organelles are challenged by the toxicity of reactive compounds, including ␣,␤-unsaturated carbonyls, which are involved in the pathophysiological effects associated with oxidative stress in cells and tissues (2). In fact, ␣,␤-unsaturated carbonyls from peroxidized polyunsaturated fatty acids cause loss of functions in mitochondria (3); chloroplasts have recently been shown to be a major production center of reactive aldehydes (4), and photosynthetic functions are highly sensitive to ␣,␤-unsaturated carbonyls (5-7).The high reactivity of ␣,␤-unsaturated carbonyls is due to the ability of their ␣,␤-unsaturated bonds to form Michael adducts with thiol and amino groups in biomolecules; in the case of ␣,␤-unsaturated aldehydes, the aldehyde group also contributes to reactivity through the formation of Schiff base adducts with amino groups. Thus the targe...

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“…In plants, very few enzymatic pathways that reduce aldehyde accumulation have been defined. Two enzymes including soybean aldose/aldehyde reductase and Arabidopsis alkenal, a, b-hydrogenase have been shown to participate in the reduction of aldehydes (Oberschall et al 2000;Mano et al 2002). In rice, two acetaldehyde-oxidizing ALDHs (ALDH1a and ALDH2a) were characterized.…”

Section: Introductionmentioning

confidence: 99%

Significant improvement of stress tolerance in tobacco plants by overexpressing a stress-responsive aldehyde dehydrogenase gene from maize (Zea mays)

Huang

Wang

et al. 2008

Plant Mol Biol

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Aldehyde dehydrogenases (ALDHs) play a central role in detoxification processes of aldehydes generated in plants when exposed to the stressed conditions. In order to identify genes required for the stresses responses in the grass crop Zea mays, an ALDH (ZmALDH22A1) gene was isolated and characterized. ZmALDH22A1 belongs to the family ALDH22 that is currently known only in plants. The ZmALDH22A1 encodes a protein of 593 amino acids that shares high identity with the orthologs from Saccharum officinarum (95%), Oryza sativa (89%), Triticum aestivum (87%) and Arabidopsis thaliana (77%), respectively. Real-time PCR analysis indicates that ZmALDH22A1 is expressed differentially in different tissues. Various elevated levels of ZmALDH22A1 expression have been detected when the seedling roots exposed to abiotic stresses including dehydration, high salinity and abscisic acid (ABA). Tomato stable transformation of construct expressing the ZmALDH22A1 signal peptide fused with yellow fluorescent protein (YFP) driven by the CaMV35S-promoter reveals that the fusion protein is targeted to plastid. Transgenic tobacco plants overexpressing ZmALDH22A1 shows elevated stresses tolerance. Stresses tolerance in transgenic plants is accompanied by a reduction of malondialdehyde (MDA) derived from cellular lipid peroxidation.

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A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses

Cited by 216 publications

References 34 publications

Environmental Stress Causes Oxidative Damage to Plant Mitochondria Leading to Inhibition of Glycine Decarboxylase

Environmental Stress Causes Oxidative Damage to Plant Mitochondria Leading to Inhibition of Glycine Decarboxylase

NADPH-dependent Reductases Involved in the Detoxification of Reactive Carbonyls in Plants

Significant improvement of stress tolerance in tobacco plants by overexpressing a stress-responsive aldehyde dehydrogenase gene from maize (Zea mays)

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