Nitric oxide-cold stress signalling cross-talk, evolution of a novel regulatory mechanism

Sehrawat, Ankita; Gupta, Ravi; Deswal, Renu

doi:10.1002/pmic.201200445

Cited by 48 publications

(33 citation statements)

References 119 publications

(198 reference statements)

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“…The present results also support the NO and cold-stress signaling model proposed in our previous review. 4 Moreover, comparison of subcellular Snitrosoproteome using literature studies showed that 82 and 65.5% targets in mitochondria 11,12 and peroxisomes, 13 respectively, were involved in the metabolic functions ( Figure S4, Supporting Information). In contrast, in the apoplast, 33% were metabolic/cell-wall-modifying and 37.5% were stress-and redox-related.…”

Section: Discussionmentioning

confidence: 98%

S-Nitrosylation Analysis in Brassica juncea Apoplast Highlights the Importance of Nitric Oxide in Cold-Stress Signaling

Sehrawat

Deswal

2014

J. Proteome Res.

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Reactive nitrogen species (RNS) including nitric oxide (NO) are important components of stress signaling. However, RNS-mediated signaling in the apoplast remains largely unknown. NO production measured in the shoot apoplast of Brassica juncea seedlings showed nonenzymatic nitrite reduction to NO. Thiol pool quantification showed cold-induced increase in the protein (including S-nitrosothiols) as well as non protein thiols. Proteins from the apoplast were resolved as 109 spots on the 2-D gel, while S-nitrosoglutathione-treated (a NO donor), neutravidin-agarose affinity chromatography-purified S-nitrosylated proteins were resolved as 52 spots. Functional categorization after MALDI-TOF/TOF identification showed 41 and 38% targets to be metabolic/cell-wall-modifying and stress-related, respectively, suggesting the potential role(s) of S-nitrosylation in regulating these responses. Additionally, identification of cold-stress-modulated putative S-nitrosylated proteins by nLC-MS/MS showed that only 38.4% targets with increased S-nitrosylation were secreted by classical pathway, while the majority (61.6%) of these were secreted by unknown/nonclassical pathways. Cold-stress-increased dehydroascorbate reductase and glutathione S-transferase activity via S-nitrosylation and promoted ROS detoxification by ascorbate regeneration and hydrogen peroxide detoxification. Taken together, cold-mediated NO production, thiol pool enrichment, and identification of the 48 putative S-nitrosylated proteins, including 25 novel targets, provided the preview of RNS-mediated cold-stress signaling in the apoplast.

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Section: Discussionmentioning

confidence: 98%

S-Nitrosylation Analysis in Brassica juncea Apoplast Highlights the Importance of Nitric Oxide in Cold-Stress Signaling

Sehrawat

Deswal

2014

J. Proteome Res.

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“…Recently, a NO-cold crosstalk was proposed at genes, lipid and protein level, but the regulatory mechanisms involved are still elusive (Sehrawat et al, 2013). Therefore, to get a better understanding of these signaling pathways, identification of the regulatory targets is essential.…”

Section: Introductionmentioning

confidence: 99%

RuBisCO depletion improved proteome coverage of cold responsive S-nitrosylated targets in Brassica juncea

Sehrawat¹,

Abat²,

Deswal³

2013

Front. Plant Sci.

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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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“…The literature describes NO responses to other abiotic stresses such as extreme temperatures, salinity, mechanical damage, UV-B, ozone, or herbicides (Gould et al, 2003; Corpas et al, 2006; Neill et al, 2008a; Molassiotis et al, 2010; Tossi et al, 2012b; Sehrawat et al, 2013; Xie et al, 2013). Although much work remains to define the physiological function of this molecule in response to abiotic stress, progress is underway.…”

Section: No and Abiotic Stressmentioning

confidence: 99%

Protein S-nitrosylation in plants under abiotic stress: an overview

2013

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Abiotic stress is one of the main problems affecting agricultural losses, and understanding the mechanisms behind plant tolerance and stress response will help us to develop new means of strengthening fruitful agronomy. The mechanisms of plant stress response are complex. Data obtained by experimental procedures are sometimes contradictory, depending on the species, strength, and timing applied. In recent years nitric oxide has been identified as a key signaling molecule involved in most plant responses to abiotic stress, either indirectly through gene activation or interaction with reactive oxygen species and hormones; or else directly, as a result of modifying enzyme activities mainly by nitration and S-nitrosylation. While the functional relevance of the S-nitrosylation of certain proteins has been assessed in response to biotic stress, it has yet to be characterized under abiotic stress. Here, we review initial works about S-nitrosylation in response to abiotic stress to conclude with a brief overview, and discuss further perspectives to obtain a clear outlook of the relevance of S-nitrosylation in plant response to abiotic stress.

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Nitric oxide-cold stress signalling cross-talk, evolution of a novel regulatory mechanism

Cited by 48 publications

References 119 publications

S-Nitrosylation Analysis in Brassica juncea Apoplast Highlights the Importance of Nitric Oxide in Cold-Stress Signaling

S-Nitrosylation Analysis in Brassica juncea Apoplast Highlights the Importance of Nitric Oxide in Cold-Stress Signaling

RuBisCO depletion improved proteome coverage of cold responsive S-nitrosylated targets in Brassica juncea

Protein S-nitrosylation in plants under abiotic stress: an overview

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