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Copper stress-induced changes in leaf soluble proteome of Cu-sensitive and tolerant Agrostis capillaris L. populations

dc.contributor.authorHEGO, E.
dc.contributor.authorVILAIN, S.
dc.contributor.authorBARRE, A.
dc.contributor.authorCLAVEROL, S.
dc.contributor.authorDUPUY, J. W.
dc.contributor.authorLALANNE, C.
dc.contributor.authorBONNEU, M.
dc.contributor.authorPLOMION, C.
dc.contributor.authorMENCH, M.
dc.date.accessioned2020-09-03T07:56:16Z
dc.date.available2020-09-03T07:56:16Z
dc.date.issued2016
dc.identifier.issn1615-9853
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10863
dc.description.abstractEnChanges in leaf soluble proteome were explored in 3-month-old plants of metallicolous (M) and nonmetallicolous (NM) Agrostis capillaris L. populations exposed to increasing Cu concentrations (1-50 mu M) to investigate molecular mechanisms underlying plant responses to Cu excess and tolerance of M plants. Plants were cultivated on perlite (CuSO4 spiked-nutrient solution). Soluble proteins, extracted by the trichloroacetic acid/acetone procedure, were separated with 2-DE (linear 4-7 pH gradient). Analysis of CCB-stained gels (PDQuest) reproducibly detected 214 spots, and 64 proteins differentially expressed were identified using LC-MS/MS. In both populations, Cu excess impacted both light-dependent (OEE, cytochrome b6-f complex, and chlorophyll a-b binding protein), and -independent (RuBisCO) photosynthesis reactions, more intensively in NM leaves (ferredoxin-NADP reductase and metalloprotease FTSH2). In both populations, upregulation of isocitrate dehydrogenase and cysteine/methionine synthases respectively suggested increased isocitrate oxidation and enhanced need for S-containing amino-acids, likely for chelation and detoxification. In NM leaves, an increasing need for energetic compounds was indicated by the stimulation of ATPases, glycolysis, pentose phosphate pathway, and Calvin cycle enzymes; impacts on protein metabolism and oxidative stress increase were respectively suggested by the rise of chaperones and redox enzymes. Overexpression of a HSP70 may be pivotal for M Cu tolerance by protecting protein metabolism. All MS data have been deposited in the ProteomeXchange with the dataset identifier PXD001930 (http//proteomecentral.proteomexchange.org/dataset/PXD001930).
dc.language.isoen
dc.title.enCopper stress-induced changes in leaf soluble proteome of Cu-sensitive and tolerant Agrostis capillaris L. populations
dc.typeArticle de revue
dc.identifier.doi10.1002/pmic.201500083
dc.subject.halChimie/Matériaux
bordeaux.journalProteomics
bordeaux.page1386-1397
bordeaux.volume16
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue9
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Proteomics&rft.date=2016&rft.volume=16&rft.issue=9&rft.spage=1386-1397&rft.epage=1386-1397&rft.eissn=1615-9853&rft.issn=1615-9853&rft.au=HEGO,%20E.&VILAIN,%20S.&BARRE,%20A.&CLAVEROL,%20S.&DUPUY,%20J.%20W.&rft.genre=article


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