The prion-like proteins have a unique biochemical memory through destructive self-organizing changes of conformation and function. They have a general biological nature, and their behavior was widely studied in mammals, bacteria, and fungi. Recently, we and other authors suggested that stress factors might cause prion-like properties in plant proteins. However, available data is preliminary and hardly convincing. Therefore, it is timely to explore if selected plant proteins, having crucial biochemical functions, such as cupins, auxin-binding proteins, RuBisCo and other photosynthetic proteins, can acquire prion-like properties due to influence of the chronic stress factors.
The aim of our study is the transition of the α-structure to β-conformation in proteins and the appearance of amyloid aggregates in plant cells challenged by suboptimal conditions under influence abiotic stress factors using state-of-the-art proteomics, microscopy, and molecular biology. Our previous studies showed that under chronic irradiation in the Chernobyl zone flax accumulates proteins with prion-like properties (Gábrišová et al., 2016). Moreover, we demonstrated with FTIR spectrometry that in X-ray-irradiated Arabidopsis thaliana transition of the α-state of proteins to β-conformation increased by 12% (Litvinov et al., 2018). Changing the conformation of proteins and increasing the relative proportion of β-sheets compared to the α-helices, which are dominant in proteins at the normal conditions, is a sign nascent of prion-like proteins in plants species.