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The measurement of the in vivo raw pH of vegetative organs is a unusual way obtaining plant knowledge. The authenticity of the pH parameter of the leaf and its independence from soil pH has already been highlighted. In the present work we observe how and to what extent water-temperature mechanisms as well as bio-fertilizers inocula can affect the raw pH and how great the biodiversity is in plants. A trial with Arabidopsis thaliana in a phytotrone has shown that, in the dark, the raw pH did not change from +18 to +35 °C (b = -0.0027 N.S.), while in the light, the regression coefficients were significant and negative, and the acidification in the leaves progressed from high (-0.0097) to normal (-0.0127) and then to low (-0.0370) water level. We have confirmed that warming induces a decrease of raw petiole pH of -0.070 pH C°-1 in grapevine leaves. In accordance with water-temperature mechanisms, the raw pH in grapevines has been found to be significantly higher in well-watered plants (pH = 4.29) than in stressed ones (4.12), with a pH decay of -3.9%. On the other hand, an average reduction of 0.10 units of raw pH would signal an increase in water stress of about -0.59 Mpa. Among the phenomena that can influence the raw pH, we have outlined three biotic factors: i) acidification as a result of a symbiotic farming fertilization i.e through the use of mycorrhizal and microbial fertilizers, with an average decay of around -3%, as a probable signature of symbiosis; ii) an “acida plantarum natura” scenario over 49 species, ranging from pH 3.06 to 6.38 ; iii) a strong (R2= 0.9) inverse polynomial pseudo-relationship of the number of fungicide sprays on the raw pH in a set of 15 species. It is suggested that this simple new multifaceted parameter can deserve interest.
GAGA-binding proteins in plants are encoded by the BARLEY B-RECOMBINANT / BASIC PENTACYSTEINE (BBR/BPC) family, which can be spilt into several groups on the basis of sequence divergence. The proteins of the different groups share an evolutionary conserved BASIC PENTACYSTEINE (BPC) domain at their very C-terminus that is important for DNA binding. Hallmark of this domain are five Cysteines at defined positions and spacing, which are considered to form a zinc-finger like structure that is involved in GAGA-motif recognition. Here, we report the formation of stabile homodimers between Arabidopsis thaliana group I member BPC1 or between group II member BPC6 in SDS-PAGE. Serial mutations of the highly conserved five Cysteines in the BPC domain of Arabidopsis thaliana BPC1 were tested for their capacity to bind to GAGA-motifs by DPI-ELISA. Our results do not support the idea of a direct involvement of these residues in making physical contact with the DNA, e.g. by formation of a zinc-finger structure. Instead, the data implies an indispensable function for the five Cysteines in homodimerization and stabilization of the protein structure by disulfide bonds. Accordingly, protein folding and structure prediction suggests the formation of a scaffold for dimerization that is supported by three intermolecular and one intramolecular S-S bond. The high degree of conservation between the BPC domains from the different groups and from different species denotes that this role for the five Cysteines might be evolutionary retained.