Protein S-nitrosylation in photosynthetic organisms: A comprehensive overview with future perspectives

Zaffagnini, Mirko; Mia, Marcello De; Morisse, Samuel; Giacinto, Nastasia Di; Marchand, Christophe; Maes, Alexandre; Lemaire, Stéphane D.; Trost, Paolo

doi:10.1016/j.bbapap.2016.02.006

Cited by 71 publications

(58 citation statements)

References 241 publications

(322 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S -nitrosylated proteins were identified from a variety of metabolic pathways including photosynthesis and light capture, the Calvin–Benson cycle and carbon capture, protein synthesis, the TCA cycle, stress response, fatty acid biosynthesis, and cell structure. Several of the S -nitrosylated proteins identified here have confirmed orthologous targets of NO in diverse organisms, including plants and algae (Zaffagnini et al, 2016). Interestingly, 80% of the S -nitrosothiols detected during active growth were undetected under nitrogen starvation (Table 1, nitrogen deplete) with only 9 of the 40 proteins identified as being S -nitrosylated during nitrogen-replete conditions still identified during nitrogen starvation conditions.…”

supporting

confidence: 52%

“…Protein S -nitrosylation by NO has been shown to play important roles in an array of cellular responses in organisms ranging from prokaryotes to metazoans. Previous studies have identified several proteins as targets of NO in higher plants, confirming S-nitrosylation as a key post-translational mechanism governing cell signaling in these organisms (Zaffagnini et al, 2016). Additional studies in the green microalga Chlamydomonas reinhardtii have identified hundreds of S -nitrosylated proteins after treatment with S -nitrosoglutathione (Samuel et al, 2014), supporting S-nitrosylation as a widespread post-translational mechanism employed by autotrophic organisms.…”

mentioning

confidence: 66%

See 1 more Smart Citation

The Chlorella vulgaris S-Nitrosoproteome under Nitrogen-Replete and -Deplete Conditions

Henard

Guarnieri

Knoshaug

2017

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

supporting

confidence: 52%

mentioning

confidence: 66%

The Chlorella vulgaris S-Nitrosoproteome under Nitrogen-Replete and -Deplete Conditions

Henard

Guarnieri

Knoshaug

2017

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

“…These RNS, like ROS, attack cellular components and require active management. Of particular importance in cyanobacteria is the reaction of NO and NO-derived species with heme proteins, iron-sulfur clusters [26], and free thiols [27, 28], which would interfere with photosynthesis and respiration, among other cellular processes.…”

Section: Introductionmentioning

confidence: 99%

Covalent attachment of the heme to Synechococcus hemoglobin alters its reactivity toward nitric oxide

Preimesberger

Johnson

Nye

et al. 2017

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

The cyanobacterium Synechococcus sp. PCC 7002 produces a monomeric hemoglobin (GlbN) implicated in the detoxification of reactive nitrogen and oxygen species. GlbN contains a b heme, which can be modified under certain reducing conditions. The modified protein (GlbN-A) has one heme–histidine C–N linkage similar to the C–S linkage of cytochrome c. No clear functional role has been assigned to this modification. Here, optical absorbance and NMR spectroscopies were used to compare the reactivity of GlbN and GlbN-A toward nitric oxide (NO). Both forms of the protein are capable of NO dioxygenase activity and both undergo heme bleaching after multiple NO challenges. GlbN and GlbN-A bind NO in the ferric state and form diamagnetic complexes (FeIII–NO) that resist reductive nitrosylation to the paramagnetic FeII–NO forms. Dithionite reduction of FeIII–NO GlbN and GlbN-A, however, resulted in distinct outcomes. Whereas GlbN-A rapidly formed the expected FeII–NO complex, NO binding to FeII GlbN caused immediate heme loss and, remarkably, was followed by slow heme rebinding and HNO (nitrosyl hydride) production. Additionally, combining FeIII GlbN, 15N-labeled nitrite, and excess dithionite resulted in the formation of FeII–H15NO GlbN. Dithionite-mediated HNO production was also observed for the related GlbN from Synechocystis sp. PCC 6803. Although ferrous GlbN-A appeared capable of trapping preformed HNO, the histidine–heme post-translational modification extinguished the NO reduction chemistry associated with GlbN. Overall, the results suggest a role for the covalent modification in FeII GlbNs: protection from NO-mediated heme loss and prevention of HNO formation.

show abstract

“…In plants, the number of identified proteins susceptible to undergo this NO-mediated modification under physiological and stress conditions, as well as how this NO-PTM could affect the function of the target proteins, is continually increasing [28][29][30][31][32][33][34][35]. Taking into consideration that this process is reversible, S-nitrosation should be assessed as a relevant mechanism of NO signal transduction in the cells.…”

Section: S-nitrosation (P-sno)mentioning

confidence: 99%

Assessing Nitric Oxide (NO) in Higher Plants: An Outline

Corpas

Palma

2018

Nitrogen

View full text Add to dashboard Cite

Nitric oxide (NO) is a free radical and a component of the N-cycle. Nevertheless, NO is likewise endogenously produced inside plant cells where it participates in a myriad of physiological functions, as well as in the mechanism of response against abiotic and biotic stresses. At biochemical level, NO has a family of derived molecules designated as reactive nitrogen species (RNS) which finally can interact with different bio-macromolecules including proteins, lipids, and nucleic acids affecting their functions. The present review has the goal to provide a comprehensive and quick overview of the relevance of NO in higher plants, especially for those researchers who are not familiar in this research area in higher plants.

show abstract

Protein S-nitrosylation in photosynthetic organisms: A comprehensive overview with future perspectives

Cited by 71 publications

References 241 publications

The Chlorella vulgaris S-Nitrosoproteome under Nitrogen-Replete and -Deplete Conditions

The Chlorella vulgaris S-Nitrosoproteome under Nitrogen-Replete and -Deplete Conditions

Covalent attachment of the heme to Synechococcus hemoglobin alters its reactivity toward nitric oxide

Assessing Nitric Oxide (NO) in Higher Plants: An Outline

Contact Info

Product

Resources

About