Chaperonins: two rings for folding

Trends Biochem Sci. 2011 Aug;36(8):424-32. doi: 10.1016/j.tibs.2011.05.003. Epub 2011 Jun 30.


Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a basic functional mechanism. Although a large amount of information has been gathered for the simpler group I, much less is known about group II chaperonins. Recent crystallographic and electron microscopy structures have provided new insights into the mechanism of these chaperonins and revealed important differences between group I and II chaperonins, mainly in the molecular rearrangements that take place during the functional cycle. These differences are evident for the most complex chaperonin, the eukaryotic cytosolic CCT, which highlights the uniqueness of this important molecular machine.

Publication types

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

MeSH terms

  • Chaperonin Containing TCP-1 / chemistry*
  • Group I Chaperonins / chemistry*
  • Group II Chaperonins / chemistry*
  • Humans
  • Models, Molecular*
  • Protein Conformation
  • Protein Folding


  • Chaperonin Containing TCP-1
  • Group I Chaperonins
  • Group II Chaperonins