How does arbuscular mycorrhizal symbiosis regulate root hydraulic properties and plasma membrane aquaporins in Phaseolus vulgaris under drought, cold or salinity stresses? New Phytol

Departamento de Microbiología del Suelo y Sistemas Simbióticos, Estación Experimental del Zaidín, CSIC, C/Profesor Alabareda 1, 18008, Granada, Spain.
New Phytologist (Impact Factor: 7.67). 02/2007; 173(4):808-16. DOI: 10.1111/j.1469-8137.2006.01961.x
Source: PubMed

ABSTRACT Here, we evaluated how the arbuscular mycorrhizal (AM) symbiosis regulates root hydraulic properties and root plasma membrane aquaporins (PIP) under different stresses sharing a common osmotic component. Phaseolus vulgaris plants were inoculated or not with the AM fungus Glomus intraradices, and subjected to drought, cold or salinity. Stress effects on root hydraulic conductance (L), PIP gene expression and protein abundance were evaluated. Under control conditions, L in AM plants was about half that in nonAM plants. However, L was decreased as a result of the three stresses in nonAM plants, while it was almost unchanged in AM plants. At the same time, PIP2 protein abundance and phosphorylation state presented the same trend as L. Finally, the expression of each PIP gene responded differently to each stress and was dependent on the AM fungal presence. Differential expression of the PIP genes studied under each stress depending on the AM fungal presence may indicate a specific function and regulation by the AM symbiosis of each gene under the specific conditions of each stress tested.

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Available from: Juan Manuel Ruiz-Lozano, Oct 29, 2014
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    • "In general, plants supply associated AM fungi with carbohydrates, and in return, fungi provide soil phosphorus (P) and possibly nitrogen (N) to their host plants (Hodge et al., 2010; Selosse and Rousset, 2011). Mycorrhizal symbioses can also provide plants with other benefits such as protection against root pathogens (Lewandowski et al., 2013) and several types of abiotic stress (Aroca et al., 2007). Furthermore, increasing evidence shows that mycorrhizas influence the structure of plant communities (Klironomos et al., 2011; Yang et al., 2014), the rhizosphere microbiome (Vestergård et al., 2008; Veresoglou et al., 2012), soil structure (van der Heijden et al., 2006; Leifheit et al., 2015), and nutrient cycles (Cheng et al., 2012; Bender et al., 2015). "
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    ABSTRACT: Abstract
    Soil Biology and Biochemistry 10/2015; 89:196-205. DOI:10.1016/j.soilbio.2015.07.007 · 4.41 Impact Factor
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    • "cognizes the phosphorylation of PIP2 proteins in a serine residue in loop B . All the antibodies were designed against the most conservative regions of these aquaporin groups ( Calvo - Polanco et al . 2014 ) . To detect PIP1 aquaporins , we used the first 26 amino acids of the N - terminal part of the PvPIP1 ; 3 protein ( accession No . DQ855475 ; Aroca et al . 2007 ) , raised as a peptide to immunize mice . To detect PIP2 aquaporins , we used the last 12 amino acids of the C - terminal part of the PvPIP2 ; 1 protein ( accession No . AY995195 ; Aroca et al . 2006 ) , raised as a peptide to immunize rabbits . To detect phosphorylated PIP2 , we used the same protein PvPIP2 ; 1 as the amino acid seque"
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    ABSTRACT: The arbuscular mycorrhizal (AM) symbiosis alters host plant physiology under drought stress, but no information is available on whether or not the AM effects respond to drought locally or systemically. A split root system was used to obtain AM plants with total or only half root system colonized, as well as, to induce physiological drought affecting the whole plant or non-physiological drought affecting only half root system. We analysed the local and/or systemic nature of the AM effects on accumulation of osmoregulatory compounds and aquaporins and on antioxidant systems. Maize plants accumulated proline both, locally in roots affected by drought and systemically when the drought affected the whole root system, being the last effect ampler in AM plants. PIPs aquaporins were also differently regulated by drought in AM and nonAM root compartments. When the drought affected only the AM root compartment, the rise of lipid peroxidation was restricted to such compartment. On the contrary, when the drought affected the nonAM root fraction, the rise of lipid peroxidation was similar in both root compartments. Thus, the benefits of the AM symbiosis not only rely in a lower oxidative stress in the host plant, it also restricts locally such oxidative stress. This article is protected by copyright. All rights reserved.
    Plant Cell and Environment 01/2015; 38(8). DOI:10.1111/pce.12507 · 5.91 Impact Factor
    • "Author's personal copy (Chaumont & Tyerman, 2014; Murai-Hatano et al., 2008), plant growth, stress responses (Vandeleur et al., 2009), and regulation of plant–water relations (Maurel et al., 2008). They are also important in symbiotic relationship such as plant–fungi interactions (Aroca, Porcel, & Ruiz-Lozano, 2007; Dietz, von Bulow, Baker, & Nehls, 2011). The functions of MIP channels are regulated in various ways. "
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    ABSTRACT: Members of the superfamily of major intrinsic proteins (MIPs) facilitate water and solute permeability across cell membranes and are found in sources ranging from bacteria to humans. Aquaporin and aquaglyceroporin channels are the prominent members of the MIP superfamily. Experimental studies show that MIPs are involved in important physiological processes in mammals and plants. They are implicated in several human diseases and are considered to be attractive drug targets for a wide range of diseases such as cancer, brain edema, epilepsy, glaucoma, and congestive heart failure. Three-dimensional structures of MIP channels from diverse sources reveal that MIPs adopt a unique conserved hourglass helical fold consisting of six transmembrane helices (TM1-TM6) and two half-helices (LB and LE). Conserved NPA motifs near the center and the aromatic/arginine selectivity filter (Ar/R SF) toward the extracellular side constitute two narrow constriction regions within the channel. Structural knowledge combined with simulation studies have helped to investigate the role of these two constriction regions in the transport and selectivity of the solutes. With the availability of many genome sequences from diverse species, a large number of MIP genes have been identified. Homology models of 1500 MIP channels have been used to derive structure-based sequence alignment of TM1-TM6 helices and the two half-helices LB and LE. Thirteen residues are highly conserved in different transmembrane helices and half-helices. High group conservation of small and weakly polar residues is observed in 27 positions at the interface of two interacting helices. Thus, although the MIP sequences are diverse, the hourglass helical fold is maintained during evolution with the conservation of these 40 positions within the transmembrane region. We have proposed a generic structure-based numbering scheme for the MIP channels that will facilitate easier comparison of the MIP sequences. Analysis of Ar/R SF in all 1500 MIPs indicates the extent of diversity in the four residues that form this narrow region. Certain residues are completely avoided in the SF, even if they have the same chemical nature as that of the most frequently observed residues. For example, arginine is the most preferred residue in a specific position of Ar/R SF, whereas lysine is almost always avoided in any of the four positions. MIP channels with highly hydrophobic or hydrophilic Ar/R SF have been identified. Similarly, there are examples of MIP channels in which all four residues of Ar/R SF are bulky, thus almost occluding the pore. Many plant MIPs possess small residues at all SF positions, resulting in a larger pore diameter. A majority of MIP channels are yet to be functionally characterized, and their in vivo substrates are not yet identified. A complete understanding of the relationship between the nature of Ar/R SF and the solutes that are transported is required to exploit MIP channels as potential drug targets. © 2015 Elsevier Inc. All rights reserved.
    Methods in enzymology 01/2015; 557:485-520. DOI:10.1016/bs.mie.2014.12.006 · 2.19 Impact Factor
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