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. 1984 Nov;81(21):6779–6783. doi: 10.1073/pnas.81.21.6779

A gene regulating the heat shock response in Escherichia coli also affects proteolysis.

T A Baker, A D Grossman, C A Gross
PMCID: PMC392015  PMID: 6387713

Abstract

The htpR locus in Escherichia coli encodes a regulator of the heat shock response. Cells containing the htpR165 mutation are defective in the induction of synthesis of heat-shock proteins at high temperature. We show that these cells are also defective in degrading two proteins that are normally unstable in htpR+ cells. The proteolytic defect is manifest at both 30 degrees C and 42 degrees C. We used a marker rescue technique to map this defect to the htpR locus. Although both proteolytic substrates are partially stabilized in lon- strains, we argue that the defect in proteolysis exhibited by the htpR165 strain does not mimic the lon- state. The htpR165 strain synthesizes Lon at the normal rate at 30 degrees C and does not show the phenotypes of mucoidy and radiation sensitivity associated with lon- strains.

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Selected References

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