A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo

J Bacteriol. 1999 Sep;181(18):5871-5. doi: 10.1128/JB.181.18.5871-5875.1999.


Chaperonins participate in the facilitated folding of a variety of proteins in vivo. To see whether the same spectrum of target proteins can be productively folded by the double-ring prokaryotic chaperonin GroEL-GroES and its single-ring human mitochondrial homolog, Hsp60-Hsp10, we expressed the latter in an Escherichia coli strain engineered so that the groE operon is under strict regulatory control. We found that expression of Hsp60-Hsp10 restores viability to cells that no longer express GroEL-GroES, formally demonstrating that Hsp60-Hsp10 can carry out all essential in vivo functions of GroEL-GroES.

Publication types

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

MeSH terms

  • Chaperonin 10 / genetics
  • Chaperonin 10 / metabolism*
  • Chaperonin 60 / genetics
  • Chaperonin 60 / metabolism*
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Genetic Engineering
  • Humans
  • Mitochondria / genetics
  • Operon
  • Recombinant Proteins / metabolism


  • Chaperonin 10
  • Chaperonin 60
  • Recombinant Proteins