Soluble and filamentous proteins in Arabidopsis sieve elements
hal.structure.identifier | Biologie du fruit et pathologie [BFP] | |
dc.contributor.author | BATAILLER, Brigitte | |
hal.structure.identifier | Institut Jean-Pierre Bourgin [IJPB] | |
dc.contributor.author | LEMAITRE, Thomas | |
hal.structure.identifier | Institut Jean-Pierre Bourgin [IJPB] | |
dc.contributor.author | VILAINE, Francoise | |
hal.structure.identifier | Ingénierie des Agro-polymères et Technologies Émergentes [UMR IATE] | |
dc.contributor.author | SANCHEZ, Christian | |
hal.structure.identifier | Unité de recherche sur les Biopolymères, Interactions Assemblages [BIA] | |
dc.contributor.author | RENARD, Denis | |
hal.structure.identifier | Institut Jean-Pierre Bourgin [IJPB] | |
dc.contributor.author | CAYLA, Thibaud | |
hal.structure.identifier | Institut Jean-Pierre Bourgin [IJPB] | |
dc.contributor.author | BENETEAU, Julie | |
hal.structure.identifier | Institut Jean-Pierre Bourgin [IJPB] | |
dc.contributor.author | DINANT, Sylvie | |
dc.date.issued | 2012 | |
dc.identifier.issn | 0140-7791 | |
dc.description.abstractEn | Phloem 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.iso | en | |
dc.publisher | Wiley | |
dc.subject.en | phloem sap | |
dc.subject.en | P-proteins | |
dc.subject.en | amino-acids | |
dc.subject.en | lectin | |
dc.subject.en | proteome | |
dc.title | Soluble and filamentous proteins in Arabidopsis sieve elements | |
dc.type | Article de revue | |
dc.identifier.doi | 10.1111/j.1365-3040.2012.02487.x | |
dc.subject.hal | Sciences du Vivant [q-bio]/Biologie végétale/Botanique | |
bordeaux.journal | Plant, Cell and Environment | |
bordeaux.page | 1258-1273 | |
bordeaux.volume | 35 | |
bordeaux.issue | 7 | |
bordeaux.peerReviewed | oui | |
hal.identifier | hal-01000336 | |
hal.version | 1 | |
hal.popular | non | |
hal.audience | Non spécifiée | |
hal.origin.link | https://hal.archives-ouvertes.fr//hal-01000336v1 | |
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