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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2008-1-30
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18165327-10092790,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1040-4651
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4120-30
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18165327-Arabidopsis,
pubmed-meshheading:18165327-Arabidopsis Proteins,
pubmed-meshheading:18165327-Chromatography, Liquid,
pubmed-meshheading:18165327-Lipid Peroxidation,
pubmed-meshheading:18165327-Models, Biological,
pubmed-meshheading:18165327-Nitrates,
pubmed-meshheading:18165327-Peroxiredoxins,
pubmed-meshheading:18165327-Peroxynitrous Acid,
pubmed-meshheading:18165327-Plants, Genetically Modified,
pubmed-meshheading:18165327-Tandem Mass Spectrometry,
pubmed-meshheading:18165327-Tyrosine
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pubmed:year |
2007
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pubmed:articleTitle |
S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration.
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pubmed:affiliation |
Dipartimento Scientifico e Tecnologico, Università degli Studi di Verona, 37134 Verona, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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