S-Nitrosylation of Peroxiredoxin II E Promotes Peroxynitrite-Mediated Tyrosine Nitration
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 kn...
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Veröffentlicht in: | The Plant cell 2007-12, Vol.19 (12), p.4120-4130 |
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Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 1040-4651 1532-298X 1532-298X |
DOI: | 10.1105/tpc.107.055061 |