The thermosome: archetype of group II chaperonins

FEBS Lett. 1998 Jun 23;430(1-2):73-7. doi: 10.1016/s0014-5793(98)00541-9.

Abstract

The thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryotes, known as TRiC or CCT, form a distinct subfamily of the chaperonins that does not depend on a co-chaperonin for protein folding activity. Recent structural data obtained by cryo- electron microscopy and X-ray crystallography provide the first insights into a novel mechanism remarkably different from that of the bacterial GroEL-GroES system.

Publication types

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

MeSH terms

  • Animals
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / classification
  • Archaeal Proteins / metabolism
  • Archaeal Proteins / physiology
  • Binding Sites
  • Chaperonin Containing TCP-1
  • Chaperonins / chemistry*
  • Chaperonins / classification
  • Chaperonins / metabolism
  • Chaperonins / physiology
  • Cytosol / metabolism
  • Eukaryotic Cells / metabolism
  • Intracellular Signaling Peptides and Proteins*
  • Microtubule-Associated Proteins*
  • Nuclear Proteins / classification
  • Protein Conformation
  • Thermosomes
  • Ubiquitin-Protein Ligases
  • t-Complex Genome Region

Substances

  • Archaeal Proteins
  • Intracellular Signaling Peptides and Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • PPP1R11 protein, human
  • Ubiquitin-Protein Ligases
  • Chaperonin Containing TCP-1
  • Chaperonins
  • Thermosomes