glycolate oxidase/nicotiana

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Glycolate oxidase gene family in Nicotiana benthamiana: genome-wide identification and functional analyses in disease resistance.

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Glycolate oxidase (GOX)-dependent production of H2O2 in response to pathogens and its function in disease resistance are still poorly understood. In this study, we performed genome-wide identification of GOX gene family in Nicotiana benthamiana and analyzed their function in various types of disease

Transcriptional and posttranscriptional regulation of the glycolate oxidase gene in tobacco seedlings.

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The roles of light and of the putative plastid signal in glycolate oxidase (GLO) gene expression were investigated in tobacco (Nicotiana tabacum cv. Samsun NN) seedlings during their shift from skotomorphogenic to photomorphogenic development. GLO transcript and enzyme activities were detected in

Structures of glycolate oxidase from Nicotiana benthamiana reveal a conserved pH sensor affecting the binding of FMN.

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Glycolate oxidase (GOX), a flavin mononucleotide (FMN)-dependent enzyme, modulates reactive oxygen species-mediated signal transduction in green plants. It has been a target protein for crop improvement because of performing a key step in photorespiration that causes the energy losses. In human, GOX

Reduction to below threshold levels of glycolate oxidase activities in transgenic tobacco enhances photoinhibition during irradiation.

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The effects of decreased flux in the glycolate pathway on photoinhibition was investigated in transgenic tobacco (Nicotiana tabacum L. cv. SR1) plants. These plants harbored a pumpkin cDNA for glycolate oxidase (GO), an enzyme in the glycolate pathway, under the control of the cauliflower mosaic

Glycolate oxidase modulates reactive oxygen species-mediated signal transduction during nonhost resistance in Nicotiana benthamiana and Arabidopsis.

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In contrast to gene-for-gene disease resistance, nonhost resistance governs defense responses to a broad range of potential pathogen species. To identify specific genes involved in the signal transduction cascade associated with nonhost disease resistance, we used a virus-induced gene-silencing

The fine structure of Cymbidium ringspot virus infections in host tissues. III. Role of peroxisomes in the genesis of multivesicular bodies.

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Ultrastructural studies of Nicotiana clevelandii plants systemically infected with Cymbidium ringspot virus, a member of the tombusvirus group, have shown that a clear-cut relationship exists between perioxisomes and multivesicular bodies (MVB). In infected cells, peroxisomes undergo a progressive

Regulation of Glycine Decarboxylase and l-Serine Hydroxymethyltransferase Activities by Glyoxylate in Tobacco Leaf Mitochondrial Preparations.

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Glyoxylate at a concentration of 10 millimolar caused 50% inhibition of decarboxylation of 20 millimolar [1-(14)C]glycine and accompanying synthesis of serine in a mitochondria-enriched preparation from tobacco (Nicotiana tabacum var. John Williams Broadleaf) leaves. None of the other compounds

Evidence for the presence in tobacco leaves of multiple enzymes for the oxidation of glycolate and glyoxylate.

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The enzymic oxidation of glycolate to glyoxylate and glyoxylate to oxalate by preparations purified from tobacco (Nicotiana tabacum var Havana Seed) leaves was studied. The K(m) values for glycolate and glyoxylate were 0.26 and 1.0 millimolar, respectively. The ratio of glycolate to glyoxylate

Enhanced Incorporation of Tritium into Glycolate during Photosynthesis by Tobacco Leaf Tissue in the Presence of Tritiated Water.

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Tobacco (Nicotiana tabacum var. Havana Seed) leaf discs were allowed to photosynthesize for 3 to 20 minutes in the presence of (14)CO(2) and (3)H(2)O. Several metabolites of the Calvin cycle and photorespiratory pathway were isolated and purified and the (3)H:(14)C values measured. Glycolate had a

Recognition of Peroxisomes by Immunofluorescence in Transformed and Untransformed Tobacco Cells.

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We report the visualization of peroxisomes in tobacco (Nicotiana tabacum) leaves using fluorescently labeled antibodies to glycolate oxidase. In transgenic tobacco leaves the expression of isocitrate lyase was also visualized. In dual probing experiments both enzymes were shown to be present

Exogenous trehalose improves growth under limiting nitrogen through upregulation of nitrogen metabolism.

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BACKGROUND The trehalose (Tre) pathway has strong effects on growth and development in plants through regulation of carbon metabolism. Altering either Tre or trehalose 6-phosphate (T6P) can improve growth and productivity of plants as observed under different water availability. As yet, there are no

The combined effect of drought stress and heat shock on gene expression in tobacco.

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In nature, plants encounter a combination of environmental conditions that may include stresses such as drought or heat shock. Although drought and heat shock have been extensively studied, little is known about how their combination affect plants. We used cDNA arrays, coupled with physiological

Synthesis of Glycolate from Pyruvate via Isocitrate Lyase by Tobacco Leaves in Light.

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Tobacco (Nicotiana tabacum var Havana Seed) leaf discs were supplied tracer quantities of [2-(14)C]- and [3-(14)C]pyruvate for 60 minutes in steady state photosynthesis with 21% or 1% O(2), and the glycolate oxidase inhibitor alpha-hydroxy-2-pyridinemethanesulfonic acid was then added for 5 or 10

Characterization of the LOV1-mediated, victorin-induced, cell-death response with virus-induced gene silencing.

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Victoria blight, caused by Cochliobolus victoriae, is a disease originally described on oat and recapitulated on Arabidopsis. C. victoriae pathogenesis depends upon production of the toxin victorin. In oat, victorin sensitivity is conferred by the Vb gene, which is genetically inseparable from the

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