Renaturation of denatured lambda repressor requires heat shock proteins

Cell. 1990 Jun 15;61(6):1013-20. doi: 10.1016/0092-8674(90)90066-n.

Abstract

The temperature-sensitive bacteriophage lambda cI857 repressor protein rapidly renatures after thermal inactivation. E. coli mutants in the heat shock protein genes dnaK, dnaJ, and grpE do not efficiently reactivate heat-denatured repressor. Our results suggest that protein refolding is promoted by heat shock proteins and that such a process is the basis of the homeostatic role played by these proteins in the heat shock response.

Publication types

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

MeSH terms

  • Bacteriophage lambda / genetics
  • Bacteriophage lambda / metabolism*
  • DNA Probes
  • DNA-Binding Proteins*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Galactokinase / metabolism
  • Genotype
  • Heat-Shock Proteins / metabolism*
  • Kinetics
  • Mutation
  • Protein Binding
  • Protein Conformation
  • Protein Denaturation
  • Repressor Proteins / metabolism*
  • Transcription Factors / metabolism*
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins

Substances

  • DNA Probes
  • DNA-Binding Proteins
  • Heat-Shock Proteins
  • Repressor Proteins
  • Transcription Factors
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • phage repressor proteins
  • Galactokinase