Molecular chaperones: inside and outside the Anfinsen cage

Curr Biol. 2001 Dec 11;11(24):R1038-40. doi: 10.1016/s0960-9822(01)00620-0.

Abstract

The GroEL/GroES chaperonin system acts as a passive anti-aggregation cage for refolding rubisco and rhodanese, and not as an active unfolding device. Refolding aconitase is too large to enter the cage but reversible binding to GroEL reduces its aggregration. Unexpectedly, confinement in the cage increases the rate of refolding of rubisco, but not rhodanese.

Publication types

  • Review

MeSH terms

  • Molecular Chaperones / metabolism*
  • Protein Folding
  • Ribulose-Bisphosphate Carboxylase / metabolism
  • Thiosulfate Sulfurtransferase / metabolism

Substances

  • Molecular Chaperones
  • Thiosulfate Sulfurtransferase
  • Ribulose-Bisphosphate Carboxylase