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The membrane proteome of Medicago truncatula roots displays qualitative and quantitative changes in response to arbuscular mycorrhizal symbiosis.

Authors :
Abdallah, Cosette
Valot, Benoit
Guillier, Christelle
Mounier, Arnaud
Balliau, Thierry
Zivy, Michel
van Tuinen, Diederik
Renaut, Jenny
Wipf, Daniel
Dumas-Gaudot, Eliane
Recorbet, Ghislaine
Source :
Journal of Proteomics. Aug2014, Vol. 108, p354-368. 15p.
Publication Year :
2014

Abstract

Arbuscular mycorrhizal (AM) symbiosis that associates roots of most land plants with soil-borne fungi (Glomeromycota), is characterized by reciprocal nutritional benefits. Fungal colonization of plant roots induces massive changes in cortical cells where the fungus differentiates an arbuscule, which drives proliferation of the plasma membrane. Despite the recognized importance of membrane proteins in sustaining AM symbiosis, the root microsomal proteome elicited upon mycorrhiza still remains to be explored. In this study, we first examined the qualitative composition of the root membrane proteome of Medicago truncatula after microsome enrichment and subsequent in depth analysis by GeLC--MS/MS. The results obtained highlighted the identification of 1226 root membrane protein candidates whose cellular and functional classifications predispose plastids and protein synthesis as prevalent organelle and function, respectively. Changes at the protein abundance level between the membrane proteomes of mycorrhizal and nonmycorrhizal roots were further monitored by spectral counting, which retrieved a total of 96 proteins that displayed a differential accumulation upon AM symbiosis. Besides the canonical markers of the periarbuscular membrane, new candidates supporting the importance of membrane trafficking events during mycorrhiza establishment/functioning were identified, including flotillin-like proteins. The data have been deposited to the ProteomeXchange with identifier PXD000875. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
18743919
Volume :
108
Database :
Academic Search Index
Journal :
Journal of Proteomics
Publication Type :
Academic Journal
Accession number :
97184908
Full Text :
https://doi.org/10.1016/j.jprot.2014.05.028