Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli

The σ(S) subunit of Escherichia coli RNA polymerase regulates the expression of stationary phase and stress response genes. σ(S) is highly unstable in exponentially growing cells, whereas its stability increases dramatically upon starvation or under certain stress conditions. The degradation of σ(S)...

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Manylion Llyfryddiaeth
Prif Awduron: Bougdour, Alexandre, Wickner, Sue, Gottesman, Susan
Fformat: Erthygl
Iaith:English
Cyhoeddwyd: Cold Spring Harbor Laboratory Press 2006
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Research Paper
Mynediad Ar-lein:https://ncbi.nlm.nih.gov/pmc/articles/PMC1472289/
https://ncbi.nlm.nih.gov/pubmed/16600914
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.1400306
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spelling pubmed-14722892006-10-01 Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli Bougdour, Alexandre Wickner, Sue Gottesman, Susan Genes Dev Research Paper The σ(S) subunit of Escherichia coli RNA polymerase regulates the expression of stationary phase and stress response genes. σ(S) is highly unstable in exponentially growing cells, whereas its stability increases dramatically upon starvation or under certain stress conditions. The degradation of σ(S) is controlled by the phosphorylatable adaptor protein RssB and the ClpXP protease. RssB specifically directs σ(S) to ClpXP. An unanswered question is how RssB-mediated degradation of σ(S) is blocked by conditions such as glucose or phosphate starvation. We report here the identification and characterization of a new regulator of σ(S) stability, IraP (inhibitor of RssB activity during phosphate starvation), that stabilizes σ(S) both in vivo and in vitro. Deletion of iraP interferes with σ(S) stabilization during phosphate starvation, but not during carbon starvation, and has a partial effect in stationary phase and nitrogen starvation. IraP interferes with RssB-dependent degradation of σ(S) through a direct protein–protein interaction with RssB. A point mutant of IraP was isolated and found to be defective both for inhibition of σ(S) degradation and interaction with RssB. Our results reveal a novel mechanism of regulation of σ(S) stability through the regulation of RssB activity and identify IraP as a member of a new class of regulators, the anti-adaptor proteins. Cold Spring Harbor Laboratory Press 2006-04-01 /pmc/articles/PMC1472289/ /pubmed/16600914 http://dx.doi.org/10.1101/gad.1400306 Text en Copyright © 2006, Cold Spring Harbor Laboratory Press
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Research Paper
spellingShingle Research Paper
Bougdour, Alexandre
Wickner, Sue
Gottesman, Susan
Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli
description The σ(S) subunit of Escherichia coli RNA polymerase regulates the expression of stationary phase and stress response genes. σ(S) is highly unstable in exponentially growing cells, whereas its stability increases dramatically upon starvation or under certain stress conditions. The degradation of σ(S) is controlled by the phosphorylatable adaptor protein RssB and the ClpXP protease. RssB specifically directs σ(S) to ClpXP. An unanswered question is how RssB-mediated degradation of σ(S) is blocked by conditions such as glucose or phosphate starvation. We report here the identification and characterization of a new regulator of σ(S) stability, IraP (inhibitor of RssB activity during phosphate starvation), that stabilizes σ(S) both in vivo and in vitro. Deletion of iraP interferes with σ(S) stabilization during phosphate starvation, but not during carbon starvation, and has a partial effect in stationary phase and nitrogen starvation. IraP interferes with RssB-dependent degradation of σ(S) through a direct protein–protein interaction with RssB. A point mutant of IraP was isolated and found to be defective both for inhibition of σ(S) degradation and interaction with RssB. Our results reveal a novel mechanism of regulation of σ(S) stability through the regulation of RssB activity and identify IraP as a member of a new class of regulators, the anti-adaptor proteins.
author Bougdour, Alexandre
Wickner, Sue
Gottesman, Susan
author_facet Bougdour, Alexandre
Wickner, Sue
Gottesman, Susan
author_sort Bougdour, Alexandre
title Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli
title_short Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli
title_full Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli
title_fullStr Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli
title_full_unstemmed Modulating RssB activity: IraP, a novel regulator of σ(S) stability in Escherichia coli
title_sort modulating rssb activity: irap, a novel regulator of σ(s) stability in escherichia coli
publisher Cold Spring Harbor Laboratory Press
publisher_facet Cold Spring Harbor Laboratory Press
publishDate 2006
url https://ncbi.nlm.nih.gov/pmc/articles/PMC1472289/
https://ncbi.nlm.nih.gov/pubmed/16600914
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.1400306
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