Plant Cell Advance Online Publication
Published on December 28, 2007; 10.1105/tpc.107.055061
OPEN ACCESS ARTICLE
Received August 15, 2007
Returned for revision October 20, 2007
Accepted November 23, 2007
S-Nitrosylation of Peroxiredoxin II E Promotes Peroxynitrite-Mediated Tyrosine Nitration
Maria C. Romero-Puertas 1, Miriam Laxa 2, Alessandro Mattè 1, Federica Zaninotto 1, Iris Finkemeier 2, Alex M.E. Jones 3, Michele Perazzolli 1, Elodie Vandelle 1, Karl-Josef Dietz 2, and Massimo Delledonne 1*
1 Dipartimento Scientifico e Tecnologico, Università degli Studi di Verona, 37134 Verona, Italy
2 Department of Plant Physiology and Biochemistry, University of Bielefeld, 33501 Bielefeld, Germany
3 Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom
* To whom correspondence should be addressed. E-mail: 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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