Heat‐shock proteins as molecular chaperones

作者：Jörg Dieter Becker, Elizabeth Anne Craig · 发表于：European Journal of Biochemistry · 年份：1994 · DOI：10.1111/j.1432-1033.1994.tb19910.x · 被引用次数：556 · 研究领域：Heat shock proteins research、Protein Structure and Dynamics、Endoplasmic Reticulum Stress and Disease

Functional proteins within cells are normally present in their native, completely folded form. However, vital processes of protein biogenesis such as protein synthesis and translocation of proteins into intracellular compartments require the protein to exist temporarily in an unfolded or partially folded conformation. As a consequence, regions buried when a polypeptide is in its native conformation become exposed and interact with other proteins causing protein aggregation which is deleterious to the cell. To prevent aggregation as proteins become unfolded, heat-shock proteins protect these interactive surfaces by binding to them and facilitating the folding of unfolded or nascent polypeptides. In other instances the binding of heat-shock proteins to interactive surfaces of completely folded proteins is a crucial part of their regulation. As heat shock and other stress conditions cause cellular proteins to become partially unfolded, the ability of heat-shock proteins to protect cells against the adverse effects of stress becomes a logical extension of their normal function as molecular chaperones.