Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

Nature. 1994 Jul 14;370(6485):111-7. doi: 10.1038/370111a0.


The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing polypeptide interacts with a specific set of molecular chaperones, including Hsp70, the DnaJ homologue Hsp40 and the chaperonin TRiC. The ordered assembly of these components on the nascent chain forms a high molecular mass complex that allows the cotranslational formation of protein domains and the completion of folding once the chain is released from the ribosome.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / physiology
  • Animals
  • Cytosol / metabolism
  • Heat-Shock Proteins / physiology*
  • In Vitro Techniques
  • Intracellular Signaling Peptides and Proteins*
  • Luciferases / metabolism
  • Microtubule-Associated Proteins*
  • Molecular Weight
  • Nuclear Proteins / physiology*
  • Peptide Chain Elongation, Translational / physiology*
  • Protein Biosynthesis / physiology
  • Protein Folding*
  • Rabbits
  • Reticulocytes / metabolism
  • Ribosomes / metabolism
  • Ubiquitin-Protein Ligases
  • t-Complex Genome Region


  • Heat-Shock Proteins
  • Intracellular Signaling Peptides and Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • Adenosine Triphosphate
  • Luciferases
  • PPP1R11 protein, human
  • Ubiquitin-Protein Ligases