In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP

FEBS Lett. 1995 Mar 13;361(1):55-60. doi: 10.1016/0014-5793(95)00151-x.

Abstract

A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg2+ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg2+ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism*
  • Chaperonin 60 / chemistry
  • Chaperonin 60 / metabolism*
  • Chloroplasts / metabolism
  • Cold Temperature
  • Escherichia coli / chemistry
  • Magnesium / metabolism
  • Mitochondria / metabolism
  • Peas
  • Protein Conformation
  • Saccharomyces cerevisiae
  • Urea / pharmacology

Substances

  • Chaperonin 60
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Urea
  • Magnesium