Heat Shock Proteins Functioning as Molecular Chaperones: Their Roles in Normal and Stressed Cells

Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29;339(1289):327-33. doi: 10.1098/rstb.1993.0031.

Abstract

In response to either elevated temperatures or several other metabolic insults, cells from all organisms respond by increasing the expression of so-called heat shock proteins (hsp or stress proteins). In general, the stress response appears to represent a universal cellular defence mechanism. The increased expression and accumulation of the stress proteins provides the cell with an added degree of protection. Studies over the past few years have revealed a role for some of the stress proteins as being intimately involved in protein maturation. Members of the hsp 70 family, distributed throughout various intracellular compartments, interact transiently with other proteins undergoing synthesis, translocation, or higher ordered assembly. Although not yet proven, it has been suggested that members of the hsp 70 family function to slow down or retard the premature folding of proteins in the course of synthesis and translocation. Yet another family of stress proteins, the hsp 60 or GroEL proteins (chaperonins), appear to function as catalysts of protein folding. Here I discuss the role of those stress proteins functioning as molecular chaperones, both within the normal cell and in the cell subjected to metabolic stress.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Chaperonin 10
  • Chaperonin 60
  • Chaperonins
  • Escherichia coli / metabolism
  • Heat-Shock Proteins / metabolism*
  • Macromolecular Substances
  • Protein Folding
  • Protein Structure, Secondary
  • Proteins / metabolism*

Substances

  • Bacterial Proteins
  • Chaperonin 10
  • Chaperonin 60
  • Heat-Shock Proteins
  • Macromolecular Substances
  • Proteins
  • Chaperonins