Physical and biochemical properties of the molecular chaperone Hsp60

Abstract

In cellular development, differentiation, and survival, the chaperone system (CS) takes center stage. The chief components of the CS are the molecular chaperones, some of which are called heat shock protein (Hsp). Hsps, together with other components of the CS, play crucial roles in assisting other proteins to fold correctly, recover from damage, and migrate across membranes, for instance. They are the unsung heroes of our cells, ensuring that everything runs smoothly. Molecular chaperones are at the front line in the response against all sorts of stressors. They have other roles besides maintaining protein homeostasis under physiological and stressful conditions (the canonical functions). The other functions are the noncanonical ones for which the CS interacts with other physiological systems, for example, the immune system. Thereby, the CS plays key roles in inflammatory and autoimmune disorders and in carcinogenesis. In this chapter, the chaperone Hsp60, also named chaperonin Hsp60, and Cpn60, is described. For this purpose, knowledge obtained with a variety of methods to generate images of atomic and molecular structures with functional roles is explained. The aim was to offer a portrait of the central character in the stories told in this book, with structural details implicated in the intramolecular movements required for functioning, and details pertinent to the intermolecular interactions also necessary for functioning. The molecular anatomy of Hsp60 and how it performs its magic while doing its various canonical and noncanonical jobs are presented.