Afficher la notice abrégée

Soluble and filamentous proteins in Arabidopsis sieve elements

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBATAILLER, Brigitte
hal.structure.identifierInstitut Jean-Pierre Bourgin [IJPB]
dc.contributor.authorLEMAITRE, Thomas
hal.structure.identifierInstitut Jean-Pierre Bourgin [IJPB]
dc.contributor.authorVILAINE, Francoise
hal.structure.identifierIngénierie des Agro-polymères et Technologies Émergentes [UMR IATE]
dc.contributor.authorSANCHEZ, Christian
hal.structure.identifierUnité de recherche sur les Biopolymères, Interactions Assemblages [BIA]
dc.contributor.authorRENARD, Denis
hal.structure.identifierInstitut Jean-Pierre Bourgin [IJPB]
dc.contributor.authorCAYLA, Thibaud
hal.structure.identifierInstitut Jean-Pierre Bourgin [IJPB]
dc.contributor.authorBENETEAU, Julie
hal.structure.identifierInstitut Jean-Pierre Bourgin [IJPB]
dc.contributor.authorDINANT, Sylvie
dc.date.issued2012
dc.identifier.issn0140-7791
dc.description.abstractEnPhloem sieve elements are highly differentiated cells involved in the long-distance transport of photoassimilates. These cells contain both aggregated phloem-proteins (P-proteins) and soluble proteins, which are also translocated by mass flow. We used liquid chromatographytandem mass spectrometry (LC-MS/MS) to carry out a proteomic survey of the phloem exudate of Arabidopsis thaliana, collected by the ethylenediaminetetraacetic acid (EDTA)-facilitated method. We identified 287 proteins, a large proportion of which were enzymes involved in the metabolic precursor generation and amino acid synthesis, suggesting that sieve tubes display high levels of metabolic activity. RNA-binding proteins, defence proteins and lectins were also found. No putative P-proteins were detected in the EDTA-exudate fraction, indicating a lack of long-distance translocation of such proteins in Arabidopsis. In parallel, we investigated the organization of P-proteins, by high-resolution transmission electron microscopy, and the localization of the phloem lectin PP2, a putative P-protein component, by immunolocalization with antibodies against PP2-A1. Transmission electron microscopy observations of P-proteins revealed bundles of filaments resembling strings of beads. PP2-A1 was found weakly associated with these structures in the sieve elements and bound to plastids. These observations suggest that PP2-A1 is anchored to P-proteins and organelles rather than being a structural component of P-proteins.
dc.language.isoen
dc.publisherWiley
dc.subject.enphloem sap
dc.subject.enP-proteins
dc.subject.enamino-acids
dc.subject.enlectin
dc.subject.enproteome
dc.titleSoluble and filamentous proteins in Arabidopsis sieve elements
dc.typeArticle de revue
dc.identifier.doi10.1111/j.1365-3040.2012.02487.x
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Botanique
bordeaux.journalPlant, Cell and Environment
bordeaux.page1258-1273
bordeaux.volume35
bordeaux.issue7
bordeaux.peerReviewedoui
hal.identifierhal-01000336
hal.version1
hal.popularnon
hal.audienceNon spécifiée
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01000336v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.title=Soluble%20and%20filamentous%20proteins%20in%20Arabidopsis%20sieve%20elements&rft.atitle=Soluble%20and%20filamentous%20proteins%20in%20Arabidopsis%20sieve%20elements&rft.jtitle=Plant,%20Cell%20and%20Environment&rft.date=2012&rft.volume=35&rft.issue=7&rft.spage=1258-1273&rft.epage=1258-1273&rft.eissn=0140-7791&rft.issn=0140-7791&rft.au=BATAILLER,%20Brigitte&LEMAITRE,%20Thomas&VILAINE,%20Francoise&SANCHEZ,%20Christian&RENARD,%20Denis&rft.genre=article


Fichier(s) constituant ce document

FichiersTailleFormatVue

Il n'y a pas de fichiers associés à ce document.

Ce document figure dans la(les) collection(s) suivante(s)

Afficher la notice abrégée