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

Abdallah, Cosette; Valot, Benoı̂t; Guillier, Christelle; Mounier, Arnaud; Balliau, Thierry; Zivy, Michel; Tuinen, Diederik van; Renaut, Jenny; Wipf, Daniel; Dumas‐Gaudot, Eliane; Recorbet, Ghislaine

doi:10.1016/j.jprot.2014.05.028

Cited by 39 publications

(38 citation statements)

References 68 publications

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“…For each replicate (n = 4) of AM and NM plants, microsome extraction from M. truncatula roots was performed at 4°C using the differential centrifugation procedure described in Abdallah et al (2014). Briefly, 100 g of roots was homogenized using a knife blender in homogenization buffer (50 mM Tris-MES, pH 8.0, 500 mM sucrose, 20 mM EDTA, 10 mM DTT, and 1 mM PMSF).…”

Section: Root Microsome Extraction and Plasma Membrane Enrichmentmentioning

confidence: 99%

“…Alpha-helical TM regions were predicted according to the Tmpred server (http://www.ch.embnet.org/software/ TMPRED_form.html), with a minimum score of 1000 (Abdallah et al 2014). N-terminal signal sequence was predicted according to the SignalP 4.0 server (http://www.cbs.…”

Section: Digital Immunoblotting and Protein Characterizationmentioning

confidence: 99%

“…The rationale behind this approach is that proteins physically associated with an organelle become enriched upon purification, while contaminants are depleted (Wiederhold et al 2010). Digital immunoblotting was then carried out on the crude microsomal fractions of M. truncatula roots using the protein list published by Abdallah et al (2014). This yielded a total of 531 microsomal proteins having a confident Arabidopsis homologue, which represented 70% (±0.6, n = 6) and 68% (±1.8, n = 6) of the total microsomal protein amount in NM and AM roots, respectively (Table S2).…”

Section: Purity Of Root Pm Fractionsmentioning

confidence: 99%

“…During the last decade, plant proteomics has been intrumental for providing a rich repertoire of protein candidates sustaining the endosymbiotic program (Valot et al 2005;Gaude et al 2012;Abdallah et al 2014), especially in the model legume Medicago truncatula that largely depends on mycorrhizas for Pi uptake (Smith et al 2009). Despite the economic importance of this legume, however, a comprehensive characterization of the root PM proteome as modified by AM fungi has not been performed.…”

Section: Introductionmentioning

confidence: 99%

“…Previous attempts to characterize the PM proteomes of mycorrhizal and nonmycorrhizal M. truncatula roots have been hindered by the lack of protein abundance measurement and incomplete genome resources (Valot et al 2006). Although, because of their hydrophobicity and relatively low abundance, the inventory of membrane proteins has lagged behind the survey of soluble proteomes, membrane proteomics has benefitted in recent years from technical advances in mass spectrometry (MS), bioinformatics resources, and label-free quantification methods (Abdallah et al 2012(Abdallah et al , 2014.…”

Section: Introductionmentioning

confidence: 99%

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The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis

Aloui¹,

Recorbet²,

Lemaître‐Guillier³

et al. 2017

Mycorrhiza

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In arbuscular mycorrhizal (AM) roots, the plasma membrane (PM) of the host plant is involved in all developmental stages of the symbiotic interaction, from initial recognition to intracellular accommodation of intra-radical hyphae and arbuscules. Although the role of the PM as the agent for cellular morphogenesis and nutrient exchange is especially accentuated in endosymbiosis, very little is known regarding the PM protein composition of mycorrhizal roots. To obtain a global overview at the proteome level of the host PM proteins as modified by symbiosis, we performed a comparative protein profiling of PM fractions from Medicago truncatula roots either inoculated or not with the AM fungus Rhizophagus irregularis. PM proteins were isolated from root microsomes using an optimized discontinuous sucrose gradient; their subsequent analysis by liquid chromatography followed by mass spectrometry (MS) identified 674 proteins. Cross-species sequence homology searches combined with MS-based quantification clearly confirmed enrichment in PM-associated proteins and depletion of major microsomal contaminants. Changes in protein amounts between the PM proteomes of mycorrhizal and non-mycorrhizal roots were monitored further by spectral counting. This workflow identified a set of 82 mycorrhiza-responsive proteins that provided insights into the plant PM response to mycorrhizal symbiosis. Among them, the association of one third of the mycorrhiza-responsive proteins with detergent-resistant membranes pointed at partitioning to PM microdomains. The PM-associated proteins responsive to mycorrhization also supported host plant control of sugar uptake to limit fungal colonization, and lipid turnover events in the PM fraction of symbiotic roots. Because of the depletion upon symbiosis of proteins mediating the replacement of phospholipids by phosphorus-free lipids in the plasmalemma, we propose a role of phosphate nutrition in the PM composition of mycorrhizal roots.

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Section: Root Microsome Extraction and Plasma Membrane Enrichmentmentioning

confidence: 99%

Section: Digital Immunoblotting and Protein Characterizationmentioning

confidence: 99%