The emergence of the chaperone machines

Trends Biochem Sci. 1992 Aug;17(8):295-9. doi: 10.1016/0968-0004(92)90439-g.

Abstract

To ensure proper polypeptide folding, oligomerization and transport, elaborate molecular 'chaperone machines' have evolved. These machines are usually composed of a major chaperone protein that binds promiscuously to nascent, unfolded, misfolded or aggregated polypeptides and a set of chaperone 'cohorts', whose function is to enhance efficiency and ensure recycling. These chaperone machines can function by themselves or synergistically to carry out their various tasks.

Publication types

  • Review

MeSH terms

  • Bacterial Proteins / metabolism
  • Chaperonins
  • Heat-Shock Proteins / metabolism
  • Homeostasis / genetics
  • Protein Folding*
  • Protein Processing, Post-Translational*
  • Proteins*

Substances

  • Bacterial Proteins
  • Heat-Shock Proteins
  • Proteins
  • SecB protein, Bacteria
  • Chaperonins