Protein S-nitrosylation: What's going on in plants?

Astier, Jérémy; Kulik, Anna; Koen, Emmanuel; Besson-Bard, Angélique; Bourque, Stéphane; Jeandroz, Sylvain; Lamotte, Olivier; Wendehenne, David

doi:10.1016/j.freeradbiomed.2012.06.032

Cited by 155 publications

(116 citation statements)

References 101 publications

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“…1 The mechanisms by which it exerts its effects are being discovered and include the mobilization of classical second messengers such as Ca 2+ and cyclic GMP, the regulation of protein kinase activities and gene expression, the modulation of lipid signaling and the post-translational modification of numerous proteins. [1][2][3][4][5] During the past 10 y, it has been recognized that NO also acts as a signaling molecule mediating iron deficiency responses. 6 Treatment with artificially-released NO was shown to improve the fitness of maize and tomato plants grown under iron deficiency.…”

Section: Introductionmentioning

confidence: 99%

Nitric oxide and glutathione impact the expression of iron uptake- and iron transport-related genes as well as the content of metals inA. thalianaplants grown under iron deficiency

Koen

Szymańska

Klinguer

et al. 2012

Plant Signaling & Behavior

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Section: Introductionmentioning

confidence: 99%

Nitric oxide and glutathione impact the expression of iron uptake- and iron transport-related genes as well as the content of metals inA. thalianaplants grown under iron deficiency

Koen

Szymańska

Klinguer

et al. 2012

Plant Signaling & Behavior

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“…1). Although S-nitrosylation may increase the catalytic activity of an enzyme (Astier et al, 2012), the chloroplast proteins studied instead showed a loss of function upon S-nitrosylation. For example, S-nitrosylation markedly decreased the activity of Rubisco, GAPDH, and DEHYDROASCORBATE REDUCTASE (Lindermayr et al, 2005).…”

Section: Tyr Nitration and S-nitrosylationmentioning

confidence: 95%

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field

2015

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Posttranslational modifications of proteins are key effectors of enzyme activity, protein interactions, targeting, and turnover rate, but despite their importance, they are still poorly understood in plants. Although numerous reports have revealed the regulatory role of protein phosphorylation in photosynthesis, various other protein modifications have been identified in chloroplasts only recently. It is known that posttranslational N a -acetylation occurs in both nuclear-and plastid-encoded chloroplast proteins, but the physiological significance of this acetylation is not yet understood. Lysine acetylation affects the localization and activity of key metabolic enzymes, and it may work antagonistically or cooperatively with lysine methylation, which also occurs in chloroplasts. In addition, tyrosine nitration may help regulate the repair cycle of photosystem II, while N-glycosylation determines enzyme activity of chloroplastic carbonic anhydrase. This review summarizes the progress in the research field of posttranslational modifications of chloroplast proteins and points out the importance of these modifications in the regulation of chloroplast metabolism.

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“…Nitric oxide can be highly toxic because it can more or less react with ROS, for example with peroxynitrite ( Figure 5) and also every pro-and antioxidant LMWM (Groß et al, 2013). Furthermore, proteome wide-scale analyses revealed that nitric oxide can nitrosylate sulfur groups besides of cysteine in proteins, which has a fundamental effect on their functions (Astier et al, 2012).…”

Section: •−mentioning

confidence: 99%

Low-molecular-weight metabolite systems chemistry

Hadaček

Bachmann

2015

Front. Environ. Sci.

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Low-molecular-weight metabolites (LMWMs) comprise primary or central and a plethora of intermediary or secondary metabolites, all of which are characterized by a molecular weight below 900 Dalton. The latter are especially prominent in sessile higher organisms, such as plants, corals, sponges and fungi, but are produced by all types of microbial organisms too. Common to all of these carbon molecules are oxygen, nitrogen and, to a lesser extent, sulfur, as heteroatoms. The latter can contribute as electron donators or acceptors to cellular redox chemistry and define the potential of the molecule to enter charge-transfer complexes. Furthermore, they allow LMWMs to serve as organic ligands in coordination complexes with various inorganic metals as central atoms. Especially the transition metals Fe, Cu, and Mn can catalyze one electron reduction of molecular oxygen, which results in formation of free radical species and reactive follow-up reaction products. As antioxidants LMWMs can scavenge free radicals. Depending on the chemical environment, the same LMWMs can act as pro-oxidants by reducing molecular oxygen. The cellular regulation of redox homeostasis, a balance between oxidation and reduction, is still far from being understood. Charge-transfer and coordination complex formation with metals shapes LMWMs into gel-like matrices in the cytosol. The quasi-polymer structure is lost usually during the isolation procedure. In the gel state, LMWMs possess semiconductor properties. Also proteins and membranes are semiconductors. Together they can represent biotransistor components that can be part of a chemoelectrical signaling system that coordinates systems chemistry by initiating cell differentiation or tissue homeostasis, the activated and the resting cell state, when it is required. This concept is not new and dates back to Albert Szent-Györgyi.

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Protein S-nitrosylation: What's going on in plants?

Cited by 155 publications

References 101 publications

Nitric oxide and glutathione impact the expression of iron uptake- and iron transport-related genes as well as the content of metals inA. thalianaplants grown under iron deficiency

Nitric oxide and glutathione impact the expression of iron uptake- and iron transport-related genes as well as the content of metals inA. thalianaplants grown under iron deficiency

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field

Low-molecular-weight metabolite systems chemistry

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