The role of heat-shock proteins as molecular chaperones

Abstract

Recent studies have revealed that protein folding and assembly events in vivo require the participation of accessory components, now being referred to as 'molecular chaperones'. A number of chaperones have been identified as members of the heat-shock (or stress) protein family. This review discusses the roles of two classes of chaperones, the heat-shock protein 70 and groEL/ES families, in facilitating protein maturation, and describes how such events are perturbed in the cell subjected to metabolic stress.