The thesis deals with cellular proteostasis – protein homeostasis, which is crucial for maintaining cell survival. It is a dynamic balance between the synthesis, folding, and degradation of cellular proteins. The main components of the proteostasis system are presented, such as molecular chaperones, the ubiquitin-proteasome system, and the lysosomal autophagy system. The proteasome is described in detail, its function in eukaryotes and prokaryotes, and the effect of aging on the efficiency of these systems. The paper highlights the links between changes in proteostasis and the onset of diseases such as Alzheimer's disease, Parkinson's disease, and cancer. As part of the thesis, we prepared recombinant subunits of the proteasome of the hyperthermophilic archaeon Aeropyrum pernix. The corresponding genes for two alpha subunits and one beta subunit of the core proteasome were amplified from the A. pernix chromosome and inserted into an expression plasmid vector for the synthesis of recombinant proteins in Escherichia coli bacteria. The synthesized proteasome subunits were partially purified from bacteria by heating the cell lysates. We showed that the alpha subunit in combination with the beta subunit degrades a simple peptide substrate at a temperature of 80 °C.
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