Differential accumulation of soluble proteins in roots of metallicolous and nonmetallicolous populations of Agrostis capillaris L. exposed to Cu
Autor: | Jean-William Dupuy, Philippe Chaumeil, Michel Mench, Frank Bedon, Elena Hego, Christophe Plomion, Marc Bonneu, Clémence M. Bes, Stéphane Claverol, Aurélien Barré, Patricia M. Palagi, Céline Lalanne |
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Přispěvatelé: | Biodiversité, Gènes & Communautés (BioGeCo), Institut National de la Recherche Agronomique (INRA)-Université de Bordeaux (UB), Swiss Institute of Bioinformatics [Lausanne] (SIB), Université de Lausanne (UNIL), Université Sciences et Technologies - Bordeaux 1, Centre Génomique Fonctionnelle, Plateforme Protéome |
Jazyk: | angličtina |
Rok vydání: | 2014 |
Předmět: |
Proteomics
0106 biological sciences Proteome [SDV]Life Sciences [q-bio] agrostis Fructose-bisphosphate aldolase Cu-tolerance Plant Roots 01 natural sciences Biochemistry Superoxide dismutase 03 medical and health sciences chemistry.chemical_compound Agrostis Electrophoresis Gel Two-Dimensional Nicotianamine Trichloroacetic acid Molecular Biology Plant Proteins 030304 developmental biology Agrostis capillaris 2. Zero hunger 0303 health sciences biology Superoxide Methylglyoxal plant proteomics biology.organism_classification Adaptation Physiological superoxide dismutase Oxidative Stress Solubility chemistry biology.protein Copper 010606 plant biology & botany |
Zdroj: | Proteomics Proteomics, Wiley-VCH Verlag, 2014, 14 (15), pp.1746-1758. ⟨10.1002/pmic.201300168⟩ |
ISSN: | 1615-9853 1615-9861 |
Popis: | International audience; Differential expression of soluble proteins was explored in roots of metallicolous (M) and non-M (NM) plants of Agrostis capillaris L. exposed to increasing Cu to partially identify molecular mechanisms underlying higher Cu tolerance in M plants. Plants were cultivated for 2 months on perlite with a CuSO4 (1–30 μM) spiked-nutrient solution. Soluble proteins extracted by the trichloroacetic acid/acetone procedure were separated with 2DE (linear 4–7 pH gradient). After Coomassie Blue staining and image analysis, 19 proteins differentially expressed were identified using LC-MS/MS and Expressed Sequence Tag (ESTs) databases. At supra-optimal Cu exposure (15–30 μM), glycolysis was likely altered in NM roots with increased production of glycerone-P and methylglyoxal based on overexpression of triosephosphate isomerase and fructose bisphosphate aldolase. Changes in tubulins and higher expressions of 5-methyltetrahydropteroyltriglutamatehomocysteine methyltransferase and S-adenosylmethionine synthase underpinned impacts on the cytoskeleton and stimulation of ethylene metabolism. Increased l-methionine and S-adenosylmethionine amounts may also facilitate production of nicotianamine, which complexes Cu, and of l-cysteine, needed for metallothioneins and GSH. In M roots, the increase of [Cu/Zn] superoxide dismutase suggested a better detoxification of superoxide, when Cu exposure rose. Higher Cu-tolerance of M plants would rather result from simultaneous cooperation of various processes than from a specific mechanism. |
Databáze: | OpenAIRE |
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