Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin

Cell. 1998 May 29;93(5):863-73. doi: 10.1016/s0092-8674(00)81446-4.


We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin. Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it. Deletion of the gene encoding a prefoldin subunit in S. cerevisiae results in a phenotype similar to those found when c-cpn is mutated, namely impaired functions of the actin and tubulin-based cytoskeleton. Consistent with prefoldin having a general role in chaperonin-mediated folding, we identify homologs in archaea, which have a class II chaperonin but contain neither actin nor tubulin. We show that by directing target proteins to chaperonin, prefoldin promotes folding in an environment in which there are many competing pathways for nonnative proteins.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Archaea / genetics
  • Biological Transport
  • Chaperonin 60 / metabolism
  • Chaperonin Containing TCP-1
  • Chaperonins / metabolism*
  • Eukaryotic Cells
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Denaturation
  • Protein Folding*
  • Rabbits
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid


  • Actins
  • Chaperonin 60
  • Molecular Chaperones
  • prefoldin
  • Chaperonin Containing TCP-1
  • Chaperonins

Associated data

  • GENBANK/Y17392
  • GENBANK/Y17393
  • GENBANK/Y17394