Coordinatore | AGENCIA ESTATAL CONSEJO SUPERIOR DE INVESTIGACIONES CIENTIFICAS
Organization address
address: CALLE SERRANO 117 contact info |
Nazionalità Coordinatore | Spain [ES] |
Totale costo | 45˙000 € |
EC contributo | 45˙000 € |
Programma | FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013) |
Code Call | FP7-PEOPLE-2007-2-2-ERG |
Funding Scheme | MC-ERG |
Anno di inizio | 2007 |
Periodo (anno-mese-giorno) | 2007-11-01 - 2010-10-31 |
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AGENCIA ESTATAL CONSEJO SUPERIOR DE INVESTIGACIONES CIENTIFICAS
Organization address
address: CALLE SERRANO 117 contact info |
ES (MADRID) | coordinator | 0.00 |
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'Peroxisomes are organelles that have an essentially oxidative type of metabolism. In plant peroxisomes the presence of proteases and a set of antioxidative enzymes have been demonstrated. In addition, the presence of nitric oxide synthase suggests that they are a cellular source of NO and adds new cellular functions to peroxisomes related to oxygen and nitrogen reactive species as they have the capacity to generate and release into the cytosol important signal molecules. The study of the regulation of these molecules that could mediate the inter-organellar communication is an important emerging area in plant research, which can supply more information on peroxisomal contribution throughout plant development and in plant response to different stress condition. Recent evidences indicate that in animal tissues NO regulates diverse biologic processes by directly modifying proteins. NO and RNS can oxidize, nitrate or nitrosylate proteins. S-nitrosylation refers to the binding of a NO group to a cysteine residue and it could play a central role in NO-mediated signalling. Accumulating data suggest that many proteins are S-nitrosylated by NO indicating that S-nitrosylation may be a ubiquitous post-translational modification regulating protein function. It has been shown that S-nitrosylation plays a comparable role to phosphorylation in animal cell biology and signal transduction. However, very little is known about the dimension of the physiological function of S-nitrosylation in plants. The aim of the proposed project is to assess the occurrence of S-nitrosylation in plant peroxisomes, with the identification and functional characterization of the NO-target proteins. Additionally, we propose the study of the changes in the pattern of S-nitrosylated proteins during different stress conditions that will help us to understand the functional consequences and the relevance of S-nitrosylation and the role of peroxisomes in physiological and pathophysiological conditions.'
European researchers have investigated the role of nitrogen oxide in plant cells. Proof that this compound is important in a plant's response to stress conditions will be a valuable tool in Europe's agricultural sector.
The search for an answer to the role of nitrogen oxide (NO) in plant cells lies in a cell body known as the peroxisome. At the heart of cell metabolism, this organelle is responsible for the production of many signal molecules that are essential for the regulation of plant development. Peroxisomes also play a major role in stress conditions such as when a plant is subjected to xenobiotics - including pollutants, ozone and the heavy metal cadmium.
The recent discovery of NO as one of the products of peroxisomes opens up the scope for their importance in plant metabolism. The precise role of NO in the peroxisome context was unclear but the fact that NO is involved in modification of protein in both animal and plant cells made the compound an exciting prospect for research by the EU- No signal project.
One of the most significant functions of NO is related to a process called s-nitrosylation. Once proteins have been produced, s-nitrosylation is responsible for changing them and is the key to plasticity in plants whereby they can change their structure and function. The process involves the attachment of NO to a certain amino acid in a protein. As such, NO could be responsible for modulation of protein activity.
For the first time, the No signal researchers observed s-nitrosylation in plant peroxisomes and identified six protein targets for this process. The plants were subjected to stresses including salt, the herbicide 2, 4-D and cadmium. The scientists also identified s-nitrosylation in the power house of the cell, the mitochondrion.
Plants are subject to many stresses through their development and have evolved a range of resistance mechanisms. Once the biochemistry behind these survival responses is clear, plant breeders can apply them to crop design to avoid loss due to disease and abiotic,non-living chemical and physical factors.