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Information × Registration Number 0222U000303, 0120U104870 , R & D reports Title Effects of stress factors on prion-like proteins synthesis in plants popup.stage_title Head Rashydov Namik M., Registration Date 05-01-2022 Organization Institute of Cell Biology and Genetic Engineering of the National Academy of Sciences of Ukraine popup.description2 Proteins with alfa- and beta-conformations in leaves and seeds of plants under the action of ionizing and UV radiation, salinity, drought and acclimation conditions by FTIR spectroscopy were determined. Proteins were isolated from the plant tissues and proteomic mass spectrometric analysis was performed to identify them in the plants under stress conditions. The probability of the appearance of prion-like properties in proteins with profiles changed under the influence of stress factors was estimated using PLAAC software. The expression levels of pea, soybean and poplar genes encoding potentially amyloid-like proteins, under the influence of stress factors – ionizing radiation, drought, salinity, was evaluated by the qPCR method. It was found that the above abiotic stresses cause statistically significant changes in the activity of studied genes. Proteins were isolated from the leaves of P. persica, and pea and barley seedlings to determine content of beta-amyloid aggregates using microscopic slides stained with Congo red. Analysis of these slides on fluorescent microscope with polarized light showed the accumulation of beta-amyloid aggregates under the action of irradiation and acclimation conditions, depending on species and phenotypic differences. It has been shown that substances of presumably polyphenolic nature that prevent beta-amyloid aggregation can be synthesized in stressed pea and P.persica plants. Proteomic and FTIR spectroscopic studies have shown the presence of "transgenerational memory" in plants associated with the prion properties of proteins. In particular, in radioresistant flax plants, which grew in exclusion zone of the Chernobyl NPP for three generations, under influence of chronic ionizing radiation, prion-like proteins were transgenerationally accumulated. Method was developed and beta-amyloid fractions from pea seeds were isolated by ultracentrifugation of SDS-treated proteins through sucrose density gradient and treatment by formic acid. Product Description popup.authors popup.nrat_date 2022-03-09 Close