Specific expression of glucose-6-phosphate dehydrogenase (G6PDH) gene by salt stress in wheat (Triticum aestivum L.)

Nemoto, Yasue; Sasakuma, Tetsuo

doi:10.1016/s0168-9452(00)00305-8

Cited by 91 publications

(70 citation statements)

References 23 publications

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“…For instance, G6PDH mRNA expression in wheat seedlings under salt stress conditions of 150 mM NaCl reached a maximum level at 12 h of the treatment (Nemoto and Sasakuma, 2000). A similar response was observed in the expression of the 6PGDH gene which was up-regulated in rice shoots under salt stress (150 mM NaCl) (Huang et al, 2003).…”

Section: Function Of Nadp-dehydrogenases Under Environmental Stress Csupporting

confidence: 58%

NADPH-generating dehydrogenases: their role in the mechanism of protection against nitro-oxidative stress induced by adverse environmental conditions

Corpas

Barroso

2014

Front. Environ. Sci.

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NADPH is an essential reductive coenzyme in biosynthetic processes such as cell growth, proliferation, and detoxification in eukaryotic cells. It is required by antioxidative systems such as the ascorbate-glutathione cycle and is also necessary for the generation of superoxide radicals by plant NADPH oxidases and for the generation of nitric oxide (NO) by L-arginine-dependent nitric oxide synthase. This coenzyme is principally re-generated by a group of NADP-dehydrogenases enzymes including glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH), both belonging to the pentose phosphate pathway, the NADP-malic enzyme (NADP-ME), and NADP-isocitrate dehydrogenase (NADP-ICDH). In this study, current perspectives on these enzymes in higher plants under different stress situations are reviewed and it is also pointed out that this group of NADPH-generating dehydrogenases is a key element in supporting the mechanism of response to nitro-oxidative stress situations.

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Section: Function Of Nadp-dehydrogenases Under Environmental Stress Csupporting

confidence: 58%

NADPH-generating dehydrogenases: their role in the mechanism of protection against nitro-oxidative stress induced by adverse environmental conditions

Corpas

Barroso

2014

Front. Environ. Sci.

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“…First, as photosynthesis is inhibited under this condition, thereby reducing the available energy sources for defense, the activation of ProDH may provide energy at the expense of Pro (Bolton, 2009). In addition, as part of the P5C-Pro cycle, ProDH may shuttle reducing equivalents to mitochondria, thus lowering the cytosolic NADPH levels required for stimulation of the oxidative pentose phosphate pathway (Hare and Cress, 1997;Nemoto and Sasakuma, 2000), a central route for the activation of disease resistance and the generation of secondary defense metabolites (Scharte et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Proline Dehydrogenase Contributes to Pathogen Defense in Arabidopsis

2011

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l-Proline (Pro) catabolism is activated in plants recovering from abiotic stresses associated with water deprivation. In this catabolic pathway, Pro is converted to glutamate by two reactions catalyzed by proline dehydrogenase (ProDH) and Ɗ1-pyrroline-5-carboxylate dehydrogenase (P5CDH), with Ɗ1-pyrroline-5-carboxylate (P5C) as the intermediate. Alternatively, under certain conditions, the P5C derived from Pro is converted back to Pro by P5C reductase, thus stimulating the Pro-P5C cycle, which may generate reactive oxygen species (ROS) as a consequence of the ProDH activity. We previously observed that Pro biosynthesis is altered in Arabidopsis (Arabidopsis thaliana) tissues that induce the hypersensitive response (HR) in response to Pseudomonas syringae. In this work, we characterized the Pro catabolic pathway and ProDH activity in this model. Induction of ProDH expression was found to be dependent on salicylic acid, and an increase in ProDH activity was detected in cells destined to die. To evaluate the role of ProDH in the HR, ProDH-silenced plants were generated. These plants displayed reduced ROS and cell death levels as well as enhanced susceptibility in response to avirulent pathogens. Interestingly, the early activation of ProDH was accompanied by an increase in P5C reductase but not in P5CDH transcripts, with few changes occurring in the Pro and P5C levels. Therefore, our results suggest that in wild-type plants, ProDH is a defense component contributing to HR and disease resistance, which apparently potentiates the accumulation of ROS. The participation of the Pro-P5C cycle in the latter response is discussed.

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“…Inhibitors of photosynthetic electron transport, such as methyl viologen, activate a plastidic isoform that is associated with the loss of phosphorylation of the protein (Hauschild and von Schaewen, 2003). Other stresses such as high salt (Nemoto and Sasakuma, 2000), fungal elicitor-induced pathogenesis response (Batz et al, 1998), and viral infection (Sindelar and Sindelarova, 2002) have been accompanied by increased activity or mRNA levels of G6PDH. Transgenic tobacco plants with decreased levels of a plastidic isoform by antisense expression showed an unexpected increase in resistance to methyl viologen (Debnam et al, 2004).…”

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confidence: 99%

Functional Analyses of Cytosolic Glucose-6-Phosphate Dehydrogenases and Their Contribution to Seed Oil Accumulation in Arabidopsis

2007

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Glucose-6-phosphate dehydrogenase (G6PDH) has been implicated in the supply of reduced nicotine amide cofactors for biochemical reactions and in modulating the redox state of cells. In plants, identification of its role is complicated due to the presence of several isoforms in the cytosol and plastids. Here we focus on G6PDHs in the cytosol of Arabidopsis (Arabidopsis thaliana) using single and double mutants disrupted in the two cytosolic G6PDHs. Only a single G6PDH isoform remained in the double mutant and was present in chloroplasts, consistent with a loss of cytosolic G6PDH activity. The activities of the cytosolic isoforms G6PD5 and G6PD6 were reciprocally increased in single mutants with no increase of their respective transcript levels. We hypothesized that G6PDH plays a role in supplying NADPH for oil accumulation in developing seeds in which photosynthesis may be light limited. G6PDH activity in seeds derived from G6PD6 and a plastid G6PDH isoform and showed a similar temporal activity pattern as oil accumulation. Seeds of the double mutant but not of the single mutants had higher oil content and increased weight compared to those of the wild type, with no alteration in the carbon to nitrogen ratio or fatty acid composition. A decrease in total G6PDH activity was observed only in the double mutant. These results suggest that loss of cytosolic G6PDH activity affects the metabolism of developing seeds by increasing carbon substrates for synthesis of storage compounds rather than by decreasing the NADPH supply specifically for fatty acid synthesis.

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Specific expression of glucose-6-phosphate dehydrogenase (G6PDH) gene by salt stress in wheat (Triticum aestivum L.)

Cited by 91 publications

References 23 publications

NADPH-generating dehydrogenases: their role in the mechanism of protection against nitro-oxidative stress induced by adverse environmental conditions

NADPH-generating dehydrogenases: their role in the mechanism of protection against nitro-oxidative stress induced by adverse environmental conditions

Proline Dehydrogenase Contributes to Pathogen Defense in Arabidopsis

Functional Analyses of Cytosolic Glucose-6-Phosphate Dehydrogenases and Their Contribution to Seed Oil Accumulation in Arabidopsis

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