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PMID: 6387713 Published · ppublish English Journal Article

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 81 ·No. 21 ·1984-11-00 ·Pages 6779-83

Baker TA, Grossman AD, Gross CA

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.

MeSH Terms
Bacterial Proteins/biosynthesis,genetics DNA, Bacterial DNA, Recombinant Escherichia coli/genetics,metabolism Genes, Bacterial Genes, Regulator Heat-Shock Proteins/biosynthesis,genetics Hot Temperature Mutation Peptide Hydrolases/genetics,metabolism Phenotype Suppression, Genetic
Chemicals
Bacterial Proteins DNA, Bacterial DNA, Recombinant Heat-Shock Proteins Peptide Hydrolases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Baker T A
Grossman A D
Gross C A
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38 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.81.21.6779
Published
1984-11-00
Pages
6779-83
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC392015
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.81.21.6779 PMC Full Text View journal details
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