Modulation of stability of the Escherichia coli heat shock regulatory factor sigma.
The heat shock response of Escherichia coli is under the positive control of the sigma 32 protein (the product of the rpoH gene). We found that overproduction of the sigma 32 protein led to concomitant overproduction of the heat shock proteins, suggesting that the intracellular sigma 32 levels limit heat shock gene expression. In support of this idea, the intracellular half-life of the sigma 32 protein synthesized from a multicopy plasmid was found to be extremely short, e.g., less than 1 min at 37 and 42 degrees C. The half-life increased progressively with a decrease in temperature, reaching 15 min at 22 degrees C. Finally, conditions known previously to increase the rate of synthesis of the heat shock proteins, i.e., a mutation in the dnaK gene or expression of phage lambda early proteins, were shown to simultaneously result in a three- to fivefold increase in the half-life of sigma 32.
Tilly
K
K
Department of Physiological Chemistry, University of Wisconsin, Madison 53706.
Spence
J
J
Georgopoulos
C
C
D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D005809:Genes, Regulator; D005838:Genotype; D006360:Heat-Shock Proteins / Q000235:genetics*; D009154:Mutation; D010641:Phenotype; D010957:Plasmids
D006360:Heat-Shock Proteins