Renaturation of denatured lambda repressor requires heat shock proteins.
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.
Gaitanaris
G A
GA
Institute of Cancer Research, College of Physicians & Surgeons, Columbia University, New York, New York 10032.
Papavassiliou
A G
AG
Rubock
P
P
Silverstein
S J
SJ
Gottesman
M E
ME
D010582:Bacteriophage lambda / Q000235:genetics / Q000378:metabolism*; D015342:DNA Probes; D004268:DNA-Binding Proteins; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005686:Galactokinase / Q000378:metabolism; D005838:Genotype; D006360:Heat-Shock Proteins / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D012097:Repressor Proteins / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins
D015342:DNA Probes; D004268:DNA-Binding Proteins; D006360:Heat-Shock Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins; D005686:Galactokinase