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
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Research Support, U.S. Gov't, P.H.S.
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Retracted Publication
MeSH terms
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Bacteriophage lambda / genetics
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Bacteriophage lambda / metabolism*
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DNA Probes
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DNA-Binding Proteins*
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Galactokinase / metabolism
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Genotype
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Heat-Shock Proteins / metabolism*
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Kinetics
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Mutation
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Protein Binding
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Protein Conformation
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Protein Denaturation
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Repressor Proteins / metabolism*
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Transcription Factors / metabolism*
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Viral Proteins
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Viral Regulatory and Accessory Proteins
Substances
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DNA Probes
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DNA-Binding Proteins
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Heat-Shock Proteins
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Repressor Proteins
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Transcription Factors
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Viral Proteins
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Viral Regulatory and Accessory Proteins
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phage repressor proteins
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Galactokinase