Source:http://linkedlifedata.com/resource/pubmed/id/19598157
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
2009-8-3
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pubmed:abstractText |
Nitric oxide and reactive oxygen species play a key role in the plant hypersensitive disease resistance response, and protein tyrosine nitration is emerging as an important mechanism of their co-operative interaction. Up to now, the proteins targeted by this post-translational modification in plants are still totally unknown. In this study, we analyzed for the first time proteins undergoing nitration during the hypersensitive response by analyzing via 1D- and 2D-western blot the protein extracts from Arabidopsis thaliana plants challenged with an avirulent bacterial pathogen (Pseudomonas syringae pv. Tomato). We show that the plant disease resistance response is correlated with a modulation of nitration of proteins involved in important cellular process, such as photosynthesis, glycolysis and nitrate assimilation. These findings shed new light on the signaling functions of nitric oxide and reactive oxygen species, paving the way on studies on the role of this post-translational modification in plants.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1522-2683
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2460-8
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pubmed:meshHeading |
pubmed-meshheading:19598157-Arabidopsis,
pubmed-meshheading:19598157-Arabidopsis Proteins,
pubmed-meshheading:19598157-Blotting, Western,
pubmed-meshheading:19598157-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:19598157-Mass Spectrometry,
pubmed-meshheading:19598157-Nitrates,
pubmed-meshheading:19598157-Nitrosation,
pubmed-meshheading:19598157-Plant Diseases,
pubmed-meshheading:19598157-Proteomics,
pubmed-meshheading:19598157-Tyrosine
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pubmed:year |
2009
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pubmed:articleTitle |
Protein nitration during defense response in Arabidopsis thaliana.
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pubmed:affiliation |
Dipartimento di Biotecnologie, University of Verona, Verona, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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