CHAPEROME: HISTORICAL PERSPECTIVE AND CURRENT CONCEPTS
Abstract
The life cycle of cells is accompanied by constant synthesis, transport and degradation of polypeptide chains — proteins and signal sequences. Each polypeptide chain has four levels of structure, and its adoption of the correct spatial conformation is necessary for the expression of the function of the molecule. Hydrophobic interactions or the formation of sulfide bridges can prevent the formation of the correct conformation. Moreover, the high-order structures of proteins are disrupted by various stress responses to the cell. In the course of studying the processes of protein synthesis and aggregation, specific highly conserved proteins were identified that can bind to a newly synthesized or damaged polypeptide, imparting a functional structure due to the sequential connection with recognition domains. These proteins are called molecular chaperones. This includes the superfamily of heat shock proteins, the synthesis of which is a nonspecific cell response to stress. To study the processes of proteostasis, it is necessary to understand that these proteins act only in close relationship with cochaperones and other auxiliary molecules. Such aggregates are called chaperomes, or chaperone machineries, and are of considerable interest in biomedical research. This review discusses the historic perspective for chaperones and chaperome as a supramolecular complex as well as their place in cell proliferation.
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