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PMID: 8550468 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease.

Journal of bacteriology ·Vol. 178 ·No. 2 ·1996-01-00 ·Pages 470-6

Schweder T, Lee KH, Lomovskaya O, Matin A

Abstract

In Escherichia coli, starvation (stationary-phase)-mediated differentiation involves 50 or more genes and is triggered by an increase in cellular sigma s levels. Western immunoblot analysis showed that in mutants lacking the protease ClpP or its cognate ATPase-containing subunit ClpX, sigma s levels of exponential-phase cells increased to those of stationary-phase wild-type cells. Lack of other potential partners of ClpP, i.e., ClpA or ClpB, or of Lon protease had no effect. In ClpXP-proficient cells, the stability of sigma s increased markedly in stationary-phase compared with exponential-phase cells, but in ClpP-deficient cells, sigma s became virtually completely stable in both phases. There was no decrease in ClpXP levels in stationary-phase wild-type cells. Thus, sigma s probably becomes more resistant to this protease in stationary phase. The reported sigma s-stabilizing effect of the hns mutation also was not due to decreased protease levels. Studies with translational fusions containing different lengths of sigma s coding region suggest that amino acid residues 173 to 188 of this sigma factor may directly or indirectly serve as at least part of the target for ClpXP protease.

MeSH Terms
ATP-Dependent Proteases ATPases Associated with Diverse Cellular Activities Adenosine Triphosphatases/genetics,physiology Bacterial Proteins/biosynthesis,genetics,metabolism Base Sequence DNA-Binding Proteins/genetics Endopeptidase Clp Escherichia coli/enzymology,genetics,physiology Escherichia coli Proteins Gene Expression Regulation, Bacterial/physiology Heat-Shock Proteins/genetics,physiology Molecular Chaperones Molecular Sequence Data Mutation Nuclear Proteins/genetics Protease La Recombinant Fusion Proteins/biosynthesis Serine Endopeptidases/genetics,physiology Sigma Factor/biosynthesis,genetics,metabolism beta-Galactosidase/biosynthesis,genetics
Chemicals
Bacterial Proteins DNA-Binding Proteins Escherichia coli Proteins H-NS protein, bacteria Heat-Shock Proteins Molecular Chaperones Nuclear Proteins Recombinant Fusion Proteins Sigma Factor sigma factor KatF protein, Bacteria beta-Galactosidase ATP-Dependent Proteases Serine Endopeptidases ClpA protease, E coli Lon protein, E coli Protease La ClpXP protease, E coli Endopeptidase Clp Adenosine Triphosphatases ClpX protein, E coli ATPases Associated with Diverse Cellular Activities
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schweder T
Department of Microbiology & Immunology, Stanford University, School of Medicine, California 94305-5402, USA.
Lee K H
Lomovskaya O
Matin A
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45 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.178.2.470-476.1996
Published
1996-01-00
Pages
470-6
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC177680
Subset
IM
Grants
NIGMS NIH HHS · IR01GM421059 · United States
External Links
PubMed source DOI: 10.1128/jb.178.2.470-476.1996 PMC Full Text View journal details
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