ABSTRACT
Studying the relationship between leaf pubescence and drought resistance is important for assessing Triticum aestivum L. genetic resources. The aim of the work was to assess resistance of common wheat genotypes with different composition and allelic state of genes that determine the leaf pubescence phenotype. We compared the drought resistance wheat variety Saratovskaya 29 (S29) with densely pubescent leaves, carrying the dominant alleles of the Hl1 and Hl3 genes, and two near isogenic lines, i: S29 hl1, hl3 and i: S29 Hl2aesp, with the introgression of the additional pubescence gene from diploid species Aegilops speltoides. Under controlled conditions of the climatic chamber, the photosynthetic pigments content, the activity of ascorbate-glutathione cycle enzymes and also the parameters of chlorophyll fluorescence used to assess the physiological state of the plants photosynthetic apparatus were studied in the leaves of S29 and the lines. Tolerance was evaluated using the comprehensive index D, calculated on the basis of the studied physiological characteristics. The recessive state of pubescence genes, as well as the introduction of the additional Hl2aesp gene, led to a 6-fold decrease in D. Under the water deficit influence, the fluorescence parameters profile changed in the lines, and the viability index decreased compared with S29. Under drought, the activity of ascorbate peroxidase, glutathione reductase and dehydroascorbate reductase in the line i: S29 hl1, hl3 decreased 1.9, 3.3 and 2.3 times, in the line i: S29 Hl2aesp it decreased 1.8, 3.6 and 1.8 times respectively, compared with S29. In a hydroponic greenhouse, line productivity was studied. Compared with S29, the thousand grains mass in the line i: S29 hl1, hl3 under water deficit was reduced. The productivity of the line i: S29 Hl2aesp was significantly reduced regardless of water supply conditions in comparison with S29. Presumably, the revealed effects are associated with violations of cross-regulatory interactions between the proteins of the trichome formation network and transcription factors that regulate plant growth and stress response.
ABSTRACT
Optically active bis-2R(-)ethylhexyl o-phthalate was obtained with 0.18% yield from dry cultured cells of Aconitum baicalense Turcz ex Rapaics 1907 by extraction with petroleum ether followed by silica gel column chromatography. Its structure was confirmed by the analysis of 13C and 1H NMR spectra. Seasonal fluctuations of quantitative phthalate content in A. baicalense cells were identified. The tests were performed under conditions excluding the presence of phthalates in reagents, materials, and laboratory dishes. The same substance was shown to be produced by cultivated cells of other plants. Biosynthesis of esters of ortho-phthalic acid by cultivated plant cells was discovered for the first time.
Subject(s)
Aconitum/chemistry , Phthalic Acids/chemistry , Plant Extracts/chemistry , Alkanes/chemistry , Carbon-13 Magnetic Resonance Spectroscopy , Cells, Cultured , Chromatography, Gel , Dibutyl Phthalate/chemistry , Dibutyl Phthalate/isolation & purification , Diterpenes , Freeze Drying , Gas Chromatography-Mass Spectrometry , Hexanes/chemistry , Indoles , Phthalic Acids/isolation & purification , Plant Extracts/isolation & purification , Proton Magnetic Resonance Spectroscopy , Silicon Dioxide , Solvents/chemistryABSTRACT
Biochemical properties of a homogenous preparation of thiol:protein disulfide oxidoreductase (TPDO, EC 1.8.4.2) isolated for the first time from mature wheat (Triticum aestivum L.) grain were studied. According to polyacrylamide gel electrophoresis data, the molecular weight of TPDO is around 167 kD, the enzyme consisting of two subunits of 77 and 73 kD, which differentiates TPDO from known enzymes of SH/SS-metabolism of wheat caryopses. In substrate specificity and enzymatic characteristics (pH and temperature optima) TPDO is similar to analogous enzymes of animal tissues. Inhibition of disulfide reductase activity by alkylating agents and heavy metal ions suggests the participation of active center SH-groups in the catalytic act and classes the enzyme as a member of the thioredoxin superfamily. The SS-reductase reduces aggregating capacity of acetic acid-soluble fraction of wheat storage proteins. The proposed physiological role of TPDO is participation in creation and regulation of SH/SS-status of wheat endosperm proteins and formation of the rheological properties of gluten.
