Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.7.1.2 (nitrate reductase)
 3,861 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Plants resistant to the fungal pathogen Leptosphaeria maculans were generated by an interspecific cross between the highly susceptible Brassica napus (canola) and the highly resistant Brassica carinata. Changes in the leaf protein profiles of these lines were investigated in order to understand the biochemical basis for the observed resistance. Two-dimensional electrophoresis followed by tandem mass spectrometry led to the identification of proteins unique to the susceptible (5 proteins) and resistant genotypes (7 proteins) as well those that were differentially expressed in the resistant genotype 48 h after challenge with the pathogen (28 proteins). Proteins identified as being unique in the resistant plant material included superoxide dismutase, nitrate reductase, and carbonic anhydrase. Photosynthetic enzymes (fructose bisphosphate aldolase, triose phosphate isomerase, sedoheptulose bisphosphatase), dehydroascorbate reductase, peroxiredoxin, malate dehydrogenase, glutamine synthetase, N-glyceraldehyde-2-phosphotransferase, and peptidyl-prolyl cis-trans isomerase were observed to be elevated in the resistant genotype upon pathogen challenge. Increased levels of the antioxidant enzyme superoxide dismutase were further validated and supported by spectrophotometric and in-gel activity assays. Other proteins identified in this study such as nitrate reductase and peptidylprolyl isomerase have not been previously described in this plant-pathogen system, and their potential involvement in an incompatible interaction is discussed.
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PMID:Proteome-level investigation of Brassica carinata-derived resistance to Leptosphaeria maculans. 1565 67

Although in the last few years good number of S-nitrosylated proteins are identified but information on endogenous targets is still limiting. Therefore, an attempt is made to decipher NO signaling in cold treated Brassica juncea seedlings. Treatment of seedlings with substrate, cofactor and inhibitor of Nitric-oxide synthase and nitrate reductase (NR), indicated NR mediated NO biosynthesis in cold. Analysis of the in vivo thiols showed depletion of low molecular weight thiols and enhancement of available protein thiols, suggesting redox changes. To have a detailed view, S-nitrosylation analysis was done using biotin switch technique (BST) and avidin-affinity chromatography. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is S-nitrosylated and therefore, is identified as target repeatedly due to its abundance. It also competes out low abundant proteins which are important NO signaling components. Therefore, RuBisCO was removed (over 80%) using immunoaffinity purification. Purified S-nitrosylated RuBisCO depleted proteins were resolved on 2-D gel as 110 spots, including 13 new, which were absent in the crude S-nitrosoproteome. These were identified by nLC-MS/MS as thioredoxin, fructose biphosphate aldolase class I, myrosinase, salt responsive proteins, peptidyl-prolyl cis-trans isomerase and malate dehydrogenase. Cold showed differential S-nitrosylation of 15 spots, enhanced superoxide dismutase activity (via S-nitrosylation) and promoted the detoxification of superoxide radicals. Increased S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase sedoheptulose-biphosphatase, and fructose biphosphate aldolase, indicated regulation of Calvin cycle by S-nitrosylation. The results showed that RuBisCO depletion improved proteome coverage and provided clues for NO signaling in cold.
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PMID:RuBisCO depletion improved proteome coverage of cold responsive S-nitrosylated targets in Brassica juncea. 2403 38