ABSTRACT
As the most widely used herbal medicine in human history and a major defence hormone in plants against a broad spectrum of pathogens and abiotic stresses, salicylic acid (SA) has attracted major research interest. With applications of modern technologies over the past 30 years, studies of the effects of SA on plant growth, development, and defence have revealed many new research frontiers and continue to deliver surprises. In this review, we provide an update on recent advances in our understanding of SA metabolism, perception, and signal transduction mechanisms in plant immunity. An overarching theme emerges that SA executes its many functions through intricate regulation at multiple steps: SA biosynthesis is regulated both locally and systemically, while its perception occurs through multiple cellular targets, including metabolic enzymes, redox regulators, transcription cofactors, and, most recently, an RNA-binding protein. Moreover, SA orchestrates a complex series of post-translational modifications of downstream signaling components and promotes the formation of biomolecular condensates that function as cellular signalling hubs. SA also impacts wider cellular functions through crosstalk with other plant hormones. Looking into the future, we propose new areas for exploration of SA functions, which will undoubtedly uncover more surprises for many years to come.
Subject(s)
Plant Immunity , Salicylic Acid , Signal Transduction , Salicylic Acid/metabolism , Plant Growth Regulators/metabolism , Gene Expression Regulation, Plant , Plants/immunology , Plants/metabolism , Plants/genetics , Plant Proteins/metabolism , Plant Proteins/geneticsABSTRACT
Proteome composition is dynamic and influenced by many internal and external cues, including developmental signals, light availability, or environmental stresses. Protein degradation, in synergy with protein biosynthesis, allows cells to respond to various stimuli and adapt by reshaping the proteome. Protein degradation mediates the final and irreversible disassembly of proteins, which is important for protein quality control and to eliminate misfolded or damaged proteins, as well as entire organelles. Consequently, it contributes to cell resilience by buffering against protein or organellar damage caused by stresses. Moreover, protein degradation plays important roles in cell signaling, as well as transcriptional and translational events. The intricate task of recognizing specific proteins for degradation is achieved by specialized systems that are tailored to the substrate's physicochemical properties and subcellular localization. These systems recognize diverse substrate cues collectively referred to as "degrons", which can assume a range of structural configurations. They are molecular surfaces recognized by E3 ligases of the ubiquitin-proteasome system, but can also be considered as general features recognized by other degradation systems, including autophagy or even organellar proteases. Here we provide an overview of the newest developments in the field, delving into the intricate processes of protein recognition and elucidating the pathways through which they are recruited for degradation.
ABSTRACT
Regulation by the small modifier SUMO is heavily dependent on spatial control of enzymes that mediate the attachment and removal of SUMO on substrate proteins. Here, we show that in the fission yeast Schizosaccharomyces pombe, delocalisation of the SUMO protease Ulp1 from the nuclear envelope results in centromeric defects that can be attributed to hyper-SUMOylation at the nuclear periphery. Unexpectedly, we find that although this localised hyper-SUMOylation impairs centromeric silencing, it can also enhance centromere clustering. Moreover, both effects are at least partially dependent on SUMOylation of the inner nuclear membrane protein Lem2. Lem2 has previously been implicated in diverse biological processes, including the promotion of both centromere clustering and silencing, but how these distinct activities are coordinated was unclear; our observations suggest a model whereby SUMOylation serves as a regulatory switch, modulating Lem2 interactions with competing partner proteins to balance its roles in alternative pathways. Our findings also reveal a previously unappreciated role for SUMOylation in promoting centromere clustering.
Subject(s)
Schizosaccharomyces pombe Proteins , Schizosaccharomyces , Schizosaccharomyces pombe Proteins/genetics , Schizosaccharomyces pombe Proteins/metabolism , Sumoylation , Nuclear Proteins/metabolism , Schizosaccharomyces/genetics , Schizosaccharomyces/metabolism , Centromere/genetics , Centromere/metabolism , Membrane Proteins/metabolism , Cluster AnalysisABSTRACT
Protein methylation is an important modulator of signal transduction pathways, but methyltransferases themselves may also be modulated. Hu et al. (2017) demonstrate in this issue of Molecular Cell that S-nitrosylation selectively modulates enzymatic activity of a protein arginine methyltransferase vital to abiotic stress tolerance.
Subject(s)
Protein-Arginine N-Methyltransferases , Signal Transduction , Arginine , MethylationABSTRACT
Hypocotyl elongation is controlled by several signals and is a major characteristic of plants growing in darkness or under warm temperature. While already several molecular mechanisms associated with this process are known, protein degradation and associated E3 ligases have hardly been studied in the context of warm temperature. In a time-course phosphoproteome analysis on Arabidopsis seedlings exposed to control or warm ambient temperature, we observed reduced levels of diverse proteins over time, which could be due to transcription, translation, and/or degradation. In addition, we observed differential phosphorylation of the LRR F-box protein SLOMO MOTION (SLOMO) at two serine residues. We demonstrate that SLOMO is a negative regulator of hypocotyl growth, also under warm temperature conditions, and protein-protein interaction studies revealed possible interactors of SLOMO, such as MKK5, DWF1, and NCED4. We identified DWF1 as a likely SLOMO substrate and a regulator of warm temperature-mediated hypocotyl growth. We propose that warm temperature-mediated regulation of SLOMO activity controls the abundance of hypocotyl growth regulators, such as DWF1, through ubiquitin-mediated degradation.
Subject(s)
Arabidopsis Proteins , Arabidopsis , F-Box Proteins , Arabidopsis/metabolism , Hypocotyl/metabolism , Arabidopsis Proteins/metabolism , Temperature , F-Box Proteins/metabolism , Gene Expression Regulation, PlantABSTRACT
Systemic acquired resistance (SAR) is a broad-spectrum plant immune response involving profound transcriptional changes that are regulated by the coactivator NPR1. Nuclear translocation of NPR1 is a critical regulatory step, but how the protein is regulated in the nucleus is unknown. Here, we show that turnover of nuclear NPR1 protein plays an important role in modulating transcription of its target genes. In the absence of pathogen challenge, NPR1 is continuously cleared from the nucleus by the proteasome, which restricts its coactivator activity to prevent untimely activation of SAR. Surprisingly, inducers of SAR promote NPR1 phosphorylation at residues Ser11/Ser15, and then facilitate its recruitment to a Cullin3-based ubiquitin ligase. Turnover of phosphorylated NPR1 is required for full induction of target genes and establishment of SAR. These in vivo data demonstrate dual roles for coactivator turnover in both preventing and stimulating gene transcription to regulate plant immunity.
Subject(s)
Arabidopsis Proteins/immunology , Arabidopsis/immunology , Arabidopsis/metabolism , Carrier Proteins/metabolism , Cell Nucleus/metabolism , Cullin Proteins , Gene Expression Regulation, Plant , Immunity, Innate , Phosphorylation , Proteasome Endopeptidase Complex/metabolism , Transcription, GeneticABSTRACT
Perception of microbes by plants leads to dynamic reprogramming of the transcriptome, which is essential for plant health. The appropriate amplitude of this transcriptional response can be regulated at multiple levels, including chromatin. However, the mechanisms underlying the interplay between chromatin remodeling and transcription dynamics upon activation of plant immunity remain poorly understood. Here, we present evidence that activation of plant immunity by bacteria leads to nucleosome repositioning, which correlates with altered transcription. Nucleosome remodeling follows distinct patterns of nucleosome repositioning at different loci. Using a reverse genetic screen, we identify multiple chromatin remodeling ATPases with previously undescribed roles in immunity, including EMBRYO SAC DEVELOPMENT ARREST 16, EDA16. Functional characterization of the immune-inducible chromatin remodeling ATPase EDA16 revealed a mechanism to negatively regulate immunity activation and limit changes in redox homeostasis. Our transcriptomic data combined with MNase-seq data for EDA16 functional knock-out and over-expressor mutants show that EDA16 selectively regulates a defined subset of genes involved in redox signaling through nucleosome repositioning. Thus, collectively, chromatin remodeling ATPases fine-tune immune responses and provide a previously uncharacterized mechanism of immune regulation.
Subject(s)
Adenosine Triphosphatases/metabolism , Arabidopsis Proteins/metabolism , Arabidopsis/physiology , Chromatin Assembly and Disassembly/immunology , DNA Helicases/metabolism , Plant Diseases/immunology , Plant Immunity/genetics , Pseudomonas syringae/immunology , Adenosine Triphosphatases/genetics , Arabidopsis/genetics , Arabidopsis/immunology , Arabidopsis Proteins/genetics , Chromatin/genetics , DNA Helicases/genetics , Homeostasis , Nucleosomes/genetics , Oxidation-Reduction , Oxidative Stress , Plant Diseases/microbiology , Nicotiana/genetics , Nicotiana/immunology , Nicotiana/physiologyABSTRACT
In eukaryotes, bursts of reactive oxygen and nitrogen species mediate cellular responses to the environment by modifying cysteines of signaling proteins. Cysteine reactivity toward nitric oxide (NO) leads to formation of S-nitrosothiols (SNOs) that play important roles in pathogenesis and immunity. However, it remains poorly understood how SNOs are employed as specific, reversible signaling cues. Here we show that in plant immunity the oxidoreductase Thioredoxin-h5 (TRXh5) reverses SNO modifications by acting as a selective protein-SNO reductase. While TRXh5 failed to restore immunity in gsnor1 mutants that display excessive accumulation of the NO donor S-nitrosoglutathione, it rescued immunity in nox1 mutants that exhibit elevated levels of free NO. Rescue by TRXh5 was conferred through selective denitrosylation of excessive protein-SNO, which reinstated signaling by the immune hormone salicylic acid. Our data indicate that TRXh5 discriminates between protein-SNO substrates to provide previously unrecognized specificity and reversibility to protein-SNO signaling in plant immunity.
Subject(s)
Arabidopsis Proteins/physiology , Arabidopsis/immunology , Plant Immunity , S-Nitrosothiols/metabolism , Thioredoxin h/physiology , Arabidopsis/genetics , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Protein Processing, Post-Translational , Signal Transduction , Thioredoxin h/genetics , Thioredoxin h/metabolismABSTRACT
SUMOylation, the covalent attachment of the small ubiquitin-like modifier (SUMO) to target proteins, is emerging as a key modulator of eukaryotic immune function. In plants, a SUMO1/2-dependent process has been proposed to control the deployment of host defense responses. The molecular mechanism underpinning this activity remains to be determined, however. Here we show that increasing nitric oxide levels following pathogen recognition promote S-nitrosylation of the Arabidopsis SUMO E2 enzyme, SCE1, at Cys139. The SUMO-conjugating activities of both SCE1 and its human homolog, UBC9, were inhibited following this modification. Accordingly, mutation of Cys139 resulted in increased levels of SUMO1/2 conjugates, disabled immune responses, and enhanced pathogen susceptibility. Our findings imply that S-nitrosylation of SCE1 at Cys139 enables NO bioactivity to drive immune activation by relieving SUMO1/2-mediated suppression. The control of global SUMOylation is thought to occur predominantly at the level of each substrate via complex local machineries. Our findings uncover a parallel and complementary mechanism by suggesting that total SUMO conjugation may also be regulated directly by SNO formation at SCE1 Cys139. This Cys is evolutionary conserved and specifically S-nitrosylated in UBC9, implying that this immune-related regulatory process might be conserved across phylogenetic kingdoms.
Subject(s)
Arabidopsis Proteins/immunology , Arabidopsis/immunology , Cysteine Endopeptidases/immunology , Nitric Oxide/immunology , Ubiquitin-Conjugating Enzymes/immunology , Arabidopsis/genetics , Arabidopsis Proteins/genetics , Cysteine Endopeptidases/genetics , Humans , Nitric Oxide/genetics , Ubiquitin-Conjugating Enzymes/geneticsABSTRACT
Regulated degradation of proteins by the 26S proteasome plays important roles in maintenance and signalling in eukaryotic cells. Proteins are marked for degradation by the action of E3 ligases that site-specifically modify their substrates by adding chains of ubiquitin. Innate immune signalling in plants is deeply reliant on the ubiquitin-26S proteasome system. While progress has been made in understanding substrate ubiquitination during plant immunity, how these substrates are processed upon arrival at the proteasome remains unclear. Here we show that specific members of the HECT domain-containing family of ubiquitin protein ligases (UPL) play important roles in proteasomal substrate processing during plant immunity. Mutations in UPL1, UPL3 and UPL5 significantly diminished immune responses activated by the immune hormone salicylic acid (SA). In depth analyses of upl3 mutants indicated that these plants were impaired in reprogramming of nearly the entire SA-induced transcriptome and failed to establish immunity against a hemi-biotrophic pathogen. UPL3 was found to physically interact with the regulatory particle of the proteasome and with other ubiquitin-26S proteasome pathway components. In agreement, we demonstrate that UPL3 enabled proteasomes to form polyubiquitin chains, thereby regulating total cellular polyubiquitination levels. Taken together, our findings suggest that proteasome-associated ubiquitin ligase activity of UPL3 promotes proteasomal processivity and is indispensable for development of plant immunity.
Subject(s)
Plant Immunity/immunology , Ubiquitin-Protein Ligase Complexes/genetics , Ubiquitin-Protein Ligases/metabolism , Arabidopsis/genetics , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Ligases/genetics , Ligases/metabolism , Plant Immunity/physiology , Polyubiquitin/genetics , Proteasome Endopeptidase Complex/genetics , Proteasome Endopeptidase Complex/metabolism , Salicylic Acid/metabolism , Ubiquitin/metabolism , Ubiquitin-Protein Ligase Complexes/metabolism , UbiquitinationABSTRACT
NPR1 (NONEXPRESSER OF PR GENES1) functions as a master regulator of the plant hormone salicylic acid (SA) signaling and plays an essential role in plant immunity. In the nucleus, NPR1 interacts with transcription factors to induce the expression of PR (PATHOGENESIS-RELATED) genes and thereby promote defense responses. However, the underlying molecular mechanism of PR gene activation is poorly understood. Furthermore, despite the importance of NPR1 in plant immunity, the regulation of NPR1 expression has not been extensively studied. Here, we show that SA promotes the interaction of NPR1 with both CDK8 (CYCLIN-DEPENDENT KINASE8) and WRKY18 (WRKY DNA-BINDING PROTEIN18) in Arabidopsis (Arabidopsis thaliana). NPR1 recruits CDK8 and WRKY18 to the NPR1 promoter, facilitating its own expression. Intriguingly, CDK8 and its associated Mediator subunits positively regulate NPR1 and PR1 expression and play a pivotal role in local and systemic immunity. Moreover, CDK8 interacts with WRKY6, WRKY18, and TGA transcription factors and brings RNA polymerase II to NPR1 and PR1 promoters and coding regions to facilitate their expression. Our studies reveal a mechanism in which NPR1 recruits CDK8, WRKY18, and TGA transcription factors along with RNA polymerase II in the presence of SA and thereby facilitates its own and target gene expression for the establishment of plant immunity.
Subject(s)
Arabidopsis Proteins/metabolism , Arabidopsis/genetics , Cyclin-Dependent Kinase 8/metabolism , Gene Expression Regulation, Plant , Plant Immunity/genetics , Salicylic Acid/metabolism , Arabidopsis/immunology , Arabidopsis/physiology , Arabidopsis Proteins/genetics , Cell Nucleus/metabolism , Cyclin-Dependent Kinase 8/genetics , Promoter Regions, Genetic/genetics , Signal Transduction , Transcription Factors/genetics , Transcription Factors/metabolism , Transcriptional ActivationABSTRACT
Cellular accumulation of reactive oxygen species (ROS) is associated with a wide range of developmental and stress responses. Although cells have evolved to use ROS as signaling molecules, their chemically reactive nature also poses a threat. Antioxidant systems are required to detoxify ROS and prevent cellular damage, but little is known about how these systems manage to function in hostile, ROS-rich environments. Here we show that during oxidative stress in plant cells, the pathogen-inducible oxidoreductase Nucleoredoxin 1 (NRX1) targets enzymes of major hydrogen peroxide (H2O2)-scavenging pathways, including catalases. Mutant nrx1 plants displayed reduced catalase activity and were hypersensitive to oxidative stress. Remarkably, catalase was maintained in a reduced state by substrate-interaction with NRX1, a process necessary for its H2O2-scavenging activity. These data suggest that unexpectedly H2O2-scavenging enzymes experience oxidative distress in ROS-rich environments and require reductive protection from NRX1 for optimal activity.
ABSTRACT
The ubiquitin-proteasome system (UPS) has been shown to play vital roles in diverse plant developmental and stress responses. The UPS post-translationally modifies cellular proteins with the small molecule ubiquitin, resulting in their regulated degradation by the proteasome. Of particular importance is the role of the UPS in regulating hormone-responsive gene expression profiles, including those triggered by the immune hormone salicylic acid (SA). SA utilizes components of the UPS pathway to reprogram the transcriptome for establishment of local and systemic immunity. Emerging evidence has shown that SA induces the activity of Cullin-RING ligases (CRLs) that fuse chains of ubiquitin to downstream transcriptional regulators and consequently target them for degradation by the proteasome. Here we review how CRL-mediated degradation of transcriptional regulators may control SA-responsive immune gene expression programmes and discuss how the UPS can be modulated by both endogenous and foreign exogenous signals. The highlighted research findings paint a clear picture of the UPS as a central hub for immune activation as well as a battle ground for hijacking by pathogens.
Subject(s)
Plant Growth Regulators/metabolism , Plant Immunity/genetics , Plant Proteins/genetics , Proteasome Endopeptidase Complex/genetics , Salicylic Acid/metabolism , Ubiquitin/genetics , Plant Proteins/metabolism , Proteasome Endopeptidase Complex/metabolism , Transcription, Genetic , Ubiquitin/metabolismABSTRACT
Salicylic acid (SA) is a plant immune signal produced after pathogen challenge to induce systemic acquired resistance. It is the only major plant hormone for which the receptor has not been firmly identified. Systemic acquired resistance in Arabidopsis requires the transcription cofactor nonexpresser of PR genes 1 (NPR1), the degradation of which acts as a molecular switch. Here we show that the NPR1 paralogues NPR3 and NPR4 are SA receptors that bind SA with different affinities. NPR3 and NPR4 function as adaptors of the Cullin 3 ubiquitin E3 ligase to mediate NPR1 degradation in an SA-regulated manner. Accordingly, the Arabidopsis npr3 npr4 double mutant accumulates higher levels of NPR1, and is insensitive to induction of systemic acquired resistance. Moreover, this mutant is defective in pathogen effector-triggered programmed cell death and immunity. Our study reveals the mechanism of SA perception in determining cell death and survival in response to pathogen challenge.
Subject(s)
Arabidopsis/genetics , Arabidopsis/metabolism , Salicylic Acid/metabolism , Signal Transduction , Arabidopsis/immunology , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Mutation , Protein Binding , Two-Hybrid System Techniques , Ubiquitin-Protein Ligases/metabolismABSTRACT
Changes in redox status are a conspicuous feature of immune responses in a variety of eukaryotes, but the associated signalling mechanisms are not well understood. In plants, attempted microbial infection triggers the rapid synthesis of nitric oxide and a parallel accumulation of reactive oxygen intermediates, the latter generated by NADPH oxidases related to those responsible for the pathogen-activated respiratory burst in phagocytes. Both nitric oxide and reactive oxygen intermediates have been implicated in controlling the hypersensitive response, a programmed execution of plant cells at sites of attempted infection. However, the molecular mechanisms that underpin their function and coordinate their synthesis are unknown. Here we show genetic evidence that increases in cysteine thiols modified using nitric oxide, termed S-nitrosothiols, facilitate the hypersensitive response in the absence of the cell death agonist salicylic acid and the synthesis of reactive oxygen intermediates. Surprisingly, when concentrations of S-nitrosothiols were high, nitric oxide function also governed a negative feedback loop limiting the hypersensitive response, mediated by S-nitrosylation of the NADPH oxidase, AtRBOHD, at Cys 890, abolishing its ability to synthesize reactive oxygen intermediates. Accordingly, mutation of Cys 890 compromised S-nitrosothiol-mediated control of AtRBOHD activity, perturbing the magnitude of cell death development. This cysteine is evolutionarily conserved and specifically S-nitrosylated in both human and fly NADPH oxidase, suggesting that this mechanism may govern immune responses in both plants and animals.
Subject(s)
Apoptosis/immunology , Arabidopsis Proteins/metabolism , Arabidopsis/immunology , Arabidopsis/microbiology , NADPH Oxidases/metabolism , Plant Cells/enzymology , Plant Cells/immunology , Plant Immunity , Animals , Arabidopsis/cytology , Arabidopsis/enzymology , Arabidopsis Proteins/chemistry , Arabidopsis Proteins/genetics , Conserved Sequence , Cysteine/chemistry , Cysteine/genetics , Cysteine/metabolism , Drosophila melanogaster , Feedback, Physiological , Humans , Mutant Proteins/chemistry , Mutant Proteins/genetics , Mutant Proteins/metabolism , Mutation , NADH, NADPH Oxidoreductases/metabolism , NADPH Oxidases/chemistry , NADPH Oxidases/genetics , Nitric Oxide/metabolism , Plant Cells/microbiology , Plant Cells/pathology , Pseudomonas syringae/immunology , Reactive Oxygen Species/metabolism , Salicylic Acid , Sulfhydryl Compounds/chemistry , Sulfhydryl Compounds/metabolismABSTRACT
Nitric oxide (NO) is emerging as a key regulator of diverse plant cellular processes. A major route for the transfer of NO bioactivity is S-nitrosylation, the addition of an NO moiety to a protein cysteine thiol forming an S-nitrosothiol (SNO). Total cellular levels of protein S-nitrosylation are controlled predominantly by S-nitrosoglutathione reductase 1 (GSNOR1) which turns over the natural NO donor, S-nitrosoglutathione (GSNO). In the absence of GSNOR1 function, GSNO accumulates, leading to dysregulation of total cellular S-nitrosylation. Here we show that endogenous NO accumulation in Arabidopsis, resulting from loss-of-function mutations in NO Overexpression 1 (NOX1), led to disabled Resistance (R) gene-mediated protection, basal resistance and defence against nonadapted pathogens. In nox1 plants both salicylic acid (SA) synthesis and signalling were suppressed, reducing SA-dependent defence gene expression. Significantly, expression of a GSNOR1 transgene complemented the SNO-dependent phenotypes of paraquat resistant 2-1 (par2-1) plants but not the NO-related characters of the nox1-1 line. Furthermore, atgsnor1-3 nox1-1 double mutants supported greater bacterial titres than either of the corresponding single mutants. Our findings imply that GSNO and NO, two pivotal redox signalling molecules, exhibit additive functions and, by extension, may have distinct or overlapping molecular targets during both immunity and development.
Subject(s)
Arabidopsis/metabolism , Nitric Oxide/metabolism , Plant Immunity , S-Nitrosoglutathione/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Disease Resistance/genetics , Gene Expression Regulation, Plant , Genes, Plant , Genetic Complementation Test , Homeostasis , Models, Biological , Mutation/genetics , Phenotype , Plants, Genetically Modified , Pseudomonas syringae/physiologyABSTRACT
In dense stands of plants, such as agricultural monocultures, plants are exposed simultaneously to competition for light and other stresses such as pathogen infection. Here, we show that both salicylic acid (SA)-dependent and jasmonic acid (JA)-dependent disease resistance is inhibited by a simultaneously reduced red:far-red light ratio (R:FR), the early warning signal for plant competition. Conversely, SA- and JA-dependent induced defences did not affect shade-avoidance responses to low R:FR. Reduced pathogen resistance by low R:FR was accompanied by a strong reduction in the regulation of JA- and SA-responsive genes. The severe inhibition of SA-responsive transcription in low R:FR appeared to be brought about by the repression of SA-inducible kinases. Phosphorylation of the SA-responsive transcription co-activator NPR1, which is required for full induction of SA-responsive transcription, was indeed reduced and may thus play a role in the suppression of SA-mediated defences by low R:FR-mediated phytochrome inactivation. Our results indicate that foraging for light through the shade-avoidance response is prioritised over plant immune responses when plants are simultaneously challenged with competition and pathogen attack.
Subject(s)
Arabidopsis Proteins/genetics , Arabidopsis/immunology , Cyclopentanes/pharmacology , Oxylipins/pharmacology , Plant Diseases/immunology , Plant Immunity , Salicylic Acid/pharmacology , Arabidopsis/drug effects , Arabidopsis/genetics , Arabidopsis/radiation effects , Arabidopsis Proteins/metabolism , Botrytis/pathogenicity , Darkness , Gene Expression , Gene Expression Profiling , Gene Expression Regulation, Plant , Light , Light Signal Transduction , Oligonucleotide Array Sequence Analysis , Phosphorylation , Phytochrome , Pseudomonas syringae/physiologyABSTRACT
Nitric oxide (NO), a gaseous, redox-active small molecule, is gradually becoming established as a central regulator of growth, development, immunity and environmental interactions in plants. A major route for the transfer of NO bioactivity is S-nitrosylation, the covalent attachment of an NO moiety to a protein cysteine thiol to form an S-nitrosothiol (SNO). This chemical transformation is rapidly emerging as a prototypic, redox-based post-translational modification integral to the life of plants. Here we review the myriad roles of NO and SNOs in plant biology and, where known, the molecular mechanisms underpining their activity.