Cytosolic Chaperonins: A Question of Promiscuity

Mol Cell. 2006 Oct 20;24(2):165-7. doi: 10.1016/j.molcel.2006.10.002.

Abstract

Chaperonins in the eukaryotic cytosol are more mysterious than their bacterial counterparts, with a heterogeneity of protein binding surfaces. In a recent issue of Molecular Cell, showed that binding specificity in the TRiC chaperonin is less than absolute and resolved the location of substrate binding surfaces in this chaperonin.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Archaeal Proteins / metabolism
  • Binding Sites
  • Chaperonin 60 / chemistry
  • Chaperonin Containing TCP-1
  • Chaperonins / metabolism
  • Chaperonins / physiology*
  • Cytoplasm / metabolism
  • Cytosol / metabolism
  • Escherichia coli / metabolism
  • Models, Biological
  • Molecular Chaperones
  • Protein Binding
  • Protein Conformation
  • Protein Folding

Substances

  • Archaeal Proteins
  • Chaperonin 60
  • Molecular Chaperones
  • Adenosine Triphosphatases
  • Chaperonin Containing TCP-1
  • Chaperonins