S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration

Romero-Puertas MC, Laxa M, Matte A, Zaninotto F, Finkemeier I, Jones AME, Perazzolli M, Vandelle E, Dietz K-J, Delledonne M (2007)
PLANT CELL 19(12): 4120-4130.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Romero-Puertas, Maria C.; Laxa, MiriamUniBi; Matte, Alessandro; Zaninotto, Federica; Finkemeier, Iris; Jones, Alex M. E.; Perazzolli, Michele; Vandelle, Elodie; Dietz, Karl-JosefUniBi; Delledonne, Massimo
Abstract / Bemerkung
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 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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Romero-Puertas MC, Laxa M, Matte A, et al. S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration. PLANT CELL. 2007;19(12):4120-4130.
Romero-Puertas, M. C., Laxa, M., Matte, A., Zaninotto, F., Finkemeier, I., Jones, A. M. E., Perazzolli, M., et al. (2007). S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration. PLANT CELL, 19(12), 4120-4130. https://doi.org/10.1105/tpc.107.055061
Romero-Puertas, Maria C., Laxa, Miriam, Matte, Alessandro, Zaninotto, Federica, Finkemeier, Iris, Jones, Alex M. E., Perazzolli, Michele, Vandelle, Elodie, Dietz, Karl-Josef, and Delledonne, Massimo. 2007. “S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration”. PLANT CELL 19 (12): 4120-4130.
Romero-Puertas, M. C., Laxa, M., Matte, A., Zaninotto, F., Finkemeier, I., Jones, A. M. E., Perazzolli, M., Vandelle, E., Dietz, K. - J., and Delledonne, M. (2007). S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration. PLANT CELL 19, 4120-4130.
Romero-Puertas, M.C., et al., 2007. S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration. PLANT CELL, 19(12), p 4120-4130.
M.C. Romero-Puertas, et al., “S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration”, PLANT CELL, vol. 19, 2007, pp. 4120-4130.
Romero-Puertas, M.C., Laxa, M., Matte, A., Zaninotto, F., Finkemeier, I., Jones, A.M.E., Perazzolli, M., Vandelle, E., Dietz, K.-J., Delledonne, M.: S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration. PLANT CELL. 19, 4120-4130 (2007).
Romero-Puertas, Maria C., Laxa, Miriam, Matte, Alessandro, Zaninotto, Federica, Finkemeier, Iris, Jones, Alex M. E., Perazzolli, Michele, Vandelle, Elodie, Dietz, Karl-Josef, and Delledonne, Massimo. “S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration”. PLANT CELL 19.12 (2007): 4120-4130.

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