S-Nitrosylation of proteins

Broillet, Marie-Christine

doi:10.1007/s000180050354

Cited by 184 publications

(140 citation statements)

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“…Recent studies have also established S-nitrosylation of protein cysteine as a major mechanism of NO regulatory signaling (reviewed in Stamler et al, 1997;Broillet, 1999;Hess et al, 2001). Protein S-nitrosylation is linked to the activity of the different NOS isoforms depending on the cell type (Gow et al, 2002).…”

Section: Protein S-nitrosylationmentioning

confidence: 99%

Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms

2003

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In the past few years, nuclear DNA damage-sensing mechanisms activated by ionizing radiation have been identified, including ATM/ATR and the DNA-dependent protein kinase. Less is known about sensing mechanisms for cytoplasmic ionization events and how these events influence nuclear processes. Several studies have demonstrated the importance of cytoplasmic signaling pathways in cytoprotection and mutagenesis. For cytoplasmic signaling, radiation-stimulated reactive oxygen species (ROS) and reactive nitrogen species (RNS) are essential activators of these pathways. This review summarizes recent studies on the chemistry of radiation-induced ROS/ RNS generation and emphasizes interactions between ROS and RNS and the relative roles of cellular ROS/ RNS generators as amplifiers of the initial ionization events. Cellular mechanisms for regulating ROS/RNS levels are discussed. The mechanisms by which cells sense ROS/RNS are examined in terms of how ROS/RNS modify protein structure and function, for example, interactions with metal-thiol clusters, protein tyrosine nitration, protein cysteine oxidation, S-thiolation and Snitrosylation. We propose that radiation-induced ROS are the initiators and that nitric oxide (NO ) or derivatives are the effectors activating these signal transduction pathways. In responding to cellular ionization events, the cell converts an oxidative signal to a nitrosative one because ROS are too reactive and unspecific in their reactions for regulatory purposes and the cell is equipped to precisely modulate NO levels.

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Section: Protein S-nitrosylationmentioning

confidence: 99%

Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms

2003

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“…Due to its redox capacity, NO is able to nitrosate many nucleophilic sites on proteins including amines, aromatic rings, alcohols and thiols. Snitrosylation is the transfer of a NO + equivalent on a free SH group of a protein leading to formation of nitrosothiol (RSNO); this reaction is fully reversible (Broillet 1999). NO can be covalently incorporated into cysteine thiols, tryptophan indols and amines, but studies of free-SH groups by radioactive SH modifying reagents, ultraviolet visible spectrometry and electro spray ionization-mass spectrometry have demonstrated that cysteine residues are rapidly nitrosylated while reactions with other amino acids occur at much slower rates, therefore formation of S-nitrosothiol bond by cysteine thiol nitrosylation is considered most important due to its reactivity under Fig.…”

Section: S-nitrosylationmentioning

confidence: 99%

S-Nitrosylation — another biological switch like phosphorylation?

Abat

Saigal

Deswal

2008

Physiol Mol Biol Plants

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Nitric oxide (NO) has emerged as a key-signaling molecule affecting plant growth and development right from seed germination to cell death. It is now being considered as a new plant hormone. NO is predominantly produced by nitric oxide synthase (NOS) in animal systems. NOS converts L-arginine (substrate) to citrulline and NO is a byproduct of the reaction. However, a similar biosynthetic mechanism is still not fully established in plants as NOS is still to be purified. First plant NOS gene (AtNOS1) was cloned from Arabidopsis suggesting the existence of NOS in plants. It was shown to be involved in hormonal signaling, stomatal closure, flowering, pathogen defense response, oxidative stress, senescence and salt tolerance. However, recent studies have raised critical questions/concerns about its substantial role in NO biosynthesis. Despite the ever increasing number of NO responses observed, little is known about the signal transduction pathway(s) and mechanisms by which NO interacts with different components and results in altered cellular activities. A brief overview is presented here. Proteins are one of the major bio-molecule besides DNA, RNA and lipids which are modified by NO and its derivatives. S-nitrosylation is a ubiquitous NO mediated posttranslational modification that might regulate broad spectrum of proteins. In this review S-nitrosylation formation, catabolism and its biological significance is discussed to present the current scenario of this modification in plants.

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“…Mechanism of Regulation HRI Activity by NO and CO-The physiological effects of NO are mediated through a number of mechanisms, including (i) S-nitrosylation of proteins (30), (ii) the generation of free radicals and oxidative stress (31), or (iii) the coordination of NO by protein-bound heme (12,32). The only known biological reactivity of CO is as a ligand for proteinbound heme, and CO is neither sulfhydryl-nor redox-active.…”

Section: Effect Of No and Co On Protein Synthesis And Eif2␣mentioning

confidence: 99%

The Heme-regulated Eukaryotic Initiation Factor 2α Kinase

Uma

Yun

Matts

2001

Journal of Biological Chemistry

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Nitric oxide (NO) has been reported to inhibit protein synthesis in eukaryotic cells by increasing the phosphorylation of the ␣-subunit of eukaryotic initiation factor (eIF) 2. However, the mechanism through which this increase occurs has not been characterized. In this report, we examined the effect of the diffusible gases nitric oxide (NO) and carbon monoxide (CO) on the activation of the heme-regulated eIF2␣ kinase (HRI) in rabbit reticulocyte lysate. Spectral analysis indicated that both NO and CO bind to the N-terminal heme-binding domain of HRI. Although NO was a very potent activator of HRI, CO markedly suppressed NO-induced HRI activation. The NO-induced activation of HRI was transduced through the interaction of NO with the N-terminal heme-binding domain of HRI and not through S-nitrosylation of HRI. We postulate that the regulation of HRI activity by diffusible gases may be of wider physiological significance, as we further demonstrate that NO generators increase eIF2␣ phosphorylation levels in NT2 neuroepithelial and C2C12 myoblast cells and activate HRI immunoadsorbed from extracts of these non-erythroid cell lines.Over 2 decades ago, the heme-regulated inhibitor (HRI) 1 of protein chain initiation in rabbit reticulocyte lysate (RRL) was identified as a heme-regulated protein kinase that phosphorylated the ␣-subunit of eukaryotic initiation factor eIF2 (reviewed in Refs. 1-3). eIF2 delivers Met-tRNA i in a complex with GTP to 43 S ribosomal initiation complexes and is released as a complex with GDP at the completion of the initiation cycle. Recycling of eIF2⅐GDP and the formation of eIF2⅐GTP⅐Met-tRNA i complexes requires the action of the guanine nucleotide exchange factor, eIF2B. Under heme-deficient conditions, HRI is activated and phosphorylates eIF2. Phosphorylated eIF2 avidly binds eIF2B, sequestering eIF2B in a poorly dissociable complex, which subsequently leads to the inhibition of the initiation of translation, as eIF2⅐GDP complexes that are present in excess of eIF2B fail to recycle. Thus, HRI functions to coordinate globin synthesis with heme availability in RRL.The amino acid sequence deduced from HRI cDNA indicates that it is composed of at least five distinct domains (4). The unique N-terminal domain of HRI contains ϳ165 amino acids. The second and fourth domains contain conserved sequence motifs I-V and motifs VI-XI, which comprise the N-terminal and C-terminal catalytic lobes of protein kinases, respectively. The third and fifth domains are also unique, consisting of ϳ140 amino acids that are inserted between the two conserved kinase lobes and ϳ50 amino acids at the C terminus, respectively.HRI is a hemoprotein that contains two distinct of hemebinding sites (5-7). Heme binding to the first site is stable, and remains associated with purified HRI, whereas heme-binding to the second site is reversible and appears to be responsible for the rapid heme-induced down-regulation of HRI activity . We have recently demonstrated that the N-terminal domain of HRI contains the stable heme-binding...

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S-Nitrosylation of proteins

Cited by 184 publications

References 50 publications

Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms

Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms

S-Nitrosylation — another biological switch like phosphorylation?

The Heme-regulated Eukaryotic Initiation Factor 2α Kinase

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