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S-Nitrosylation of Peroxiredoxin II E Promotes Peroxynitrite-Mediated Tyrosine Nitration
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S-Nitrosylation of Peroxiredoxin II E Promotes Peroxynitrite-Mediated Tyrosine Nitration
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Journal Article
S-Nitrosylation of Peroxiredoxin II E Promotes Peroxynitrite-Mediated Tyrosine Nitration
2007
Overview
Nitric oxide (NO) is a free radical product of cell metabolism that plays diverse and important roles in the regulation of cellular function. S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification for the transduction of NO bioactivity, but very little is known about its physiological functions in plants. We investigated the molecular mechanism for S-nitrosylation of peroxiredoxin II E (PrxII E) from Arabidopsis thaliana and found that this posttranslational modification inhibits the hydroperoxide-reducing peroxidase activity of PrxII E, thus revealing a novel regulatory mechanism for peroxiredoxins. Furthermore, we obtained biochemical and genetic evidence that PrxII E functions in detoxifying peroxynitrite (ONOO⁻), a potent oxidizing and nitrating species formed in a diffusion-limited reaction between NO and$\\text{O}_{2}{}^{-}$that can interfere with Tyr kinase signaling through the nitration of Tyr residues. S-Nitrosylation also inhibits the ONOO⁻ detoxification activity of PrxII E, causing a dramatic increase of ONOO⁻-dependent nitrotyrosine residue formation. The same increase was observed in a prxII E mutant line after exposure to ONOO⁻, indicating that the PrxII E modulation of ONOO⁻ bioactivity is biologically relevant. We conclude that NO regulates the effects of its own radicals through the S-nitrosylation of crucial components of the antioxidant defense system that function as common triggers for reactive oxygen species- and NO-mediated signaling events.
Publisher
American Society of Plant Biologists
Subject
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Gels
/ genetics
/ Leaves
/ Lipids
/ Nitrates
/ Nitrogen
/ Oxides
/ Peroxynitrous Acid - chemistry
/ Peroxynitrous Acid - metabolism
/ phospholipid-hydroperoxide glutathione peroxidase
/ Plants
/ Plants, Genetically Modified
/ post-translational modification
/ tyrosine
