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PMID: 7724592 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 92 ·No. 8 ·1995-04-11 ·Pages 3516-20

Herman C, Thévenet D, D'Ari R, Bouloc P

Abstract

The heat shock response in Escherichia coli is governed by the concentration of the highly unstable sigma factor sigma 32. The essential protein HflB (FtsH), known to control proteolysis of the phage lambda cII protein, also governs sigma 32 degradation: an HflB-depleted strain accumulated sigma 32 and induced the heat shock response, and the half-life of sigma 32 increased by a factor up to 12 in mutants with reduced HflB function and decreased by a factor of 1.8 in a strain overexpressing HflB. The hflB gene is in the ftsJ-hflB operon, one promoter of which is positively regulated by heat shock and sigma 32. The lambda cIII protein, which stabilizes sigma 32 and lambda cII, appears to inhibit the HflB-governed protease. The E. coli HflB protein controls the stability of two master regulators, lambda cII and sigma 32, responsible for the lysis-lysogeny decision of phage lambda and the heat shock response of the host.

Related Genes
hflB
MeSH Terms
ATP-Dependent Proteases Adenosine Triphosphatases/metabolism Bacterial Proteins/metabolism Base Sequence Endopeptidases/metabolism Escherichia coli/growth & development,metabolism Escherichia coli Proteins Gene Expression Regulation, Bacterial Half-Life Heat-Shock Proteins/metabolism Lysogeny/genetics Membrane Proteins/metabolism Models, Genetic Molecular Sequence Data Promoter Regions, Genetic Sigma Factor/metabolism Transcription Factors/metabolism Viral Proteins
Chemicals
Bacterial Proteins Escherichia coli Proteins Heat-Shock Proteins Membrane Proteins Sigma Factor Transcription Factors Viral Proteins cII protein, bacteriophage lambda cIII protein, Bacteriophage lambda heat-shock sigma factor 32 Endopeptidases ATP-Dependent Proteases FtsH protein, E coli Adenosine Triphosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Herman C
Institut Jacques Monod, Centre National de la Recherche Scientifique, Université Paris, France.
Thévenet D
D'Ari R
Bouloc P
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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.92.8.3516
Published
1995-04-11
Pages
3516-20
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC42198
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.92.8.3516 PMC Full Text View journal details
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