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S-nitroso-proteome in poplar leaves in response to acute ozone stress.

PLoS ONE 9:e106886 (2014)
Publ. Version/Full Text DOI
Open Access Gold
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Protein S-nitrosylation, the covalent binding of nitric oxide (NO) to protein cysteine residues, is one of the main mechanisms of NO signaling in plant and animal cells. Using a combination of the biotin switch assay and label-free LC-MS/MS analysis, we revealed the S-nitroso-proteome of the woody model plant Populus x canescens. Under normal conditions, constitutively S-nitrosylated proteins in poplar leaves and calli comprise all aspects of primary and secondary metabolism. Acute ozone fumigation was applied to elicit ROS-mediated changes of the S-nitroso-proteome. This treatment changed the total nitrite and nitrosothiol contents of poplar leaves and affected the homeostasis of 32 S-nitrosylated proteins. Multivariate data analysis revealed that ozone exposure negatively affected the S-nitrosylation status of leaf proteins: 23 proteins were de-nitrosylated and 9 proteins had increased S-nitrosylation content compared to the control. Phenylalanine ammonia-lyase 2 (log2[ozone/control] = -3.6) and caffeic acid O-methyltransferase (-3.4), key enzymes catalyzing important steps in the phenylpropanoid and subsequent lignin biosynthetic pathways, respectively, were de-nitrosylated upon ozone stress. Measuring the in vivo and in vitro phenylalanine ammonia-lyase activity indicated that the increase of the phenylalanine ammonia-lyase activity in response to acute ozone is partly regulated by de-nitrosylation, which might favor a higher metabolic flux through the phenylpropanoid pathway within minutes after ozone exposure.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Phenylalanine Ammonia-lyase; Nitric-oxide Production; Induced Cell-death; Biochemical-plant Responses; False Discovery Rate; Arabidopsis-thaliana; Nitrosylated Proteins; Abiotic Stress; Glyceraldehyde-3-phosphate Dehydrogenase; Carboxylase/oxygenase Activity
ISSN (print) / ISBN 1932-6203
Journal PLoS ONE
Quellenangaben Volume: 9, Issue: 9, Pages: , Article Number: e106886 Supplement: ,
Publisher Public Library of Science (PLoS)
Publishing Place Lawrence, Kan.
Reviewing status Peer reviewed