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S-Nitrosylation of Peroxiredoxin II E Promotes Peroxynitrite-Mediated Tyrosine Nitration^[W],[OA]

^a Dipartimento Scientifico e Tecnologico, Università degli Studi di Verona, 37134 Verona, Italy
^b Department of Plant Physiology and Biochemistry, University of Bielefeld, 33501 Bielefeld, Germany
^c Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom

⁵ Address correspondence to massimo.delledonne{at}univr.it.

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 O₂^– 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.

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