Summary• At least three fungal 'networks' are formed in ectomycorrhizal symbiosis: the Hartig net, the sheath and extramatrical hyphae. Since these structures have different functions regarding uptake, storage and partitioning of carbohydrates and nutrients, regulation and coordination of metabolic fluxes are of special interest for ectomycorrhizal functioning.• To get some insight into structure-specific functions, the Amanita fungal sheath was separated by microdissection from the remaining Populus roots that still contained the Hartig net. Expression of the genes coding for phenylalanine ammonium lyase ( AmPAL ) and hexose transporter ( AmMst1 ) was investigated separately for both structures by RT-PCR.• When constitutively expressed fungal genes were used as a control, the expression of AmMst1 was enhanced about six-fold in hyphae of the Hartig net compared with those of the fungal sheath. By contrast, AmPAL was only barely detectable in the Hartig net, but highly expressed in the fungal sheath.• Since in pure fungal culture both genes are regulated by monosaccharides, it is supposed that an apoplastic hexose gradient, between hyphae of the Hartig net and those of the fungal sheath, might regulate fungal gene expression and thus hyphal physiology within ectomycorrhizas.
In the soils of mature forests, nitrogen availability is mainly the result of litter decomposition. Thus protein degradation is of major interest for nutrition. Two aspartic proteases were excreted in a pH-dependent manner by the ectomycorrhizal fungus Amanita muscaria grown in liquid culture. AmProt1 with a molecular mass of approximately 45 kDa was mainly present at pH values up to 5·4, whereas the excretion of AmProt2 with a molecular mass of about 90 kDa was only detectable at pH values between pH 5·4 and 6·3. In addition, the pH optima of both enzymes differed significantly. AmProt1 had a narrow pH optimum around 3, whereas AmProt2 had a broad pH optimum between 3 and 5·5 and a higher affinity to the substrate methylcasein. One cDNA-clone ( AmProt1 *) that presumably encodes AmProt1 was identified. Like AmProt1, this cDNA was expressed in a pH-dependent manner. In addition, carbohydrate and to a lesser extent nitrogen depletion significantly enhanced AmProt1 * expression. In fully developed Populus hyb./ A. muscaria ectomycorrhizas the expression of AmProt1 * was significantly higher in hyphae of the Hartig net compared with those of the fungal sheath. The role of AmProt1 and AmProt2 for fungal physiology and competitiveness is discussed.
NON-PHOTOTROPIC HYPOCOTYL 3 (NPH3) is a key component of the auxin-dependent plant phototropic growth response. We report that NPH3 directly binds polyacidic phospholipids, required for plasma membrane association in darkness. We further demonstrate that blue light induces an immediate phosphorylation of a C-terminal 14-3-3 binding motif in NPH3. Subsequent association of 14-3-3 proteins is causal for the light-induced release of NPH3 from the membrane and accompanied by NPH3 dephosphorylation. In the cytosol, NPH3 dynamically transitions into membraneless condensate-like structures. The dephosphorylated state of the 14-3-3 binding site and NPH3 membrane recruitment are recoverable in darkness. NPH3 variants that constitutively localize either to the membrane or to condensates are non-functional, revealing a fundamental role of the 14-3-3 mediated dynamic change in NPH3 localization for auxin-dependent phototropism. This regulatory mechanism might be of general nature, given that several members of the NPH3-like family interact with 14-3-3 via a C-terminal motif.
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