The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.

<h4>Background</h4>Among the seven different sigma factors in E. coli σ(70) has the highest concentration and affinity for the core RNA polymerase. The E. coli protein Rsd is regarded as an anti-sigma factor, inhibiting σ(70)-dependent transcription at the onset of stationary growth. Alt...

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Autores principales:	Nina Hofmann, Reinhild Wurm, Rolf Wagner
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2f4a584b40fe4fab90b3be6dc478be3a
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spelling	oai:doaj.org-article:2f4a584b40fe4fab90b3be6dc478be3a2021-11-18T06:54:22ZThe E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.1932-620310.1371/journal.pone.0019235https://doaj.org/article/2f4a584b40fe4fab90b3be6dc478be3a2011-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21573101/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Among the seven different sigma factors in E. coli σ(70) has the highest concentration and affinity for the core RNA polymerase. The E. coli protein Rsd is regarded as an anti-sigma factor, inhibiting σ(70)-dependent transcription at the onset of stationary growth. Although binding of Rsd to σ(70) has been shown and numerous structural studies on Rsd have been performed the detailed mechanism of action is still unknown.<h4>Methodology/principal findings</h4>We have performed studies to unravel the function and regulation of Rsd expression in vitro and in vivo. Cross-linking and affinity binding revealed that Rsd is able to interact with σ(70), with the core enzyme of RNA polymerase and is able to form dimers in solution. Unexpectedly, we find that Rsd does also interact with σ(38), the stationary phase-specific sigma factor. This interaction was further corroborated by gel retardation and footprinting studies with different promoter fragments and σ(38)- or σ(70)-containing RNA polymerase in presence of Rsd. Under competitive in vitro transcription conditions, in presence of both sigma factors, a selective inhibition of σ(70)-dependent transcription was prevailing, however. Analysis of rsd expression revealed that the nucleoid-associated proteins H-NS and FIS, StpA and LRP bind to the regulatory region of the rsd promoters. Furthermore, the major promoter P2 was shown to be down-regulated in vivo by RpoS, the stationary phase-specific sigma factor and the transcription factor DksA, while induction of the stringent control enhanced rsd promoter activity. Most notably, the dam-dependent methylation of a cluster of GATC sites turned out to be important for efficient rsd transcription.<h4>Conclusions/significance</h4>The results contribute to a better understanding of the intricate mechanism of Rsd-mediated sigma factor specificity changes during stationary phase.Nina HofmannReinhild WurmRolf WagnerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 5, p e19235 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nina Hofmann Reinhild Wurm Rolf Wagner The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.
description	<h4>Background</h4>Among the seven different sigma factors in E. coli σ(70) has the highest concentration and affinity for the core RNA polymerase. The E. coli protein Rsd is regarded as an anti-sigma factor, inhibiting σ(70)-dependent transcription at the onset of stationary growth. Although binding of Rsd to σ(70) has been shown and numerous structural studies on Rsd have been performed the detailed mechanism of action is still unknown.<h4>Methodology/principal findings</h4>We have performed studies to unravel the function and regulation of Rsd expression in vitro and in vivo. Cross-linking and affinity binding revealed that Rsd is able to interact with σ(70), with the core enzyme of RNA polymerase and is able to form dimers in solution. Unexpectedly, we find that Rsd does also interact with σ(38), the stationary phase-specific sigma factor. This interaction was further corroborated by gel retardation and footprinting studies with different promoter fragments and σ(38)- or σ(70)-containing RNA polymerase in presence of Rsd. Under competitive in vitro transcription conditions, in presence of both sigma factors, a selective inhibition of σ(70)-dependent transcription was prevailing, however. Analysis of rsd expression revealed that the nucleoid-associated proteins H-NS and FIS, StpA and LRP bind to the regulatory region of the rsd promoters. Furthermore, the major promoter P2 was shown to be down-regulated in vivo by RpoS, the stationary phase-specific sigma factor and the transcription factor DksA, while induction of the stringent control enhanced rsd promoter activity. Most notably, the dam-dependent methylation of a cluster of GATC sites turned out to be important for efficient rsd transcription.<h4>Conclusions/significance</h4>The results contribute to a better understanding of the intricate mechanism of Rsd-mediated sigma factor specificity changes during stationary phase.
format	article
author	Nina Hofmann Reinhild Wurm Rolf Wagner
author_facet	Nina Hofmann Reinhild Wurm Rolf Wagner
author_sort	Nina Hofmann
title	The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.
title_short	The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.
title_full	The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.
title_fullStr	The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.
title_full_unstemmed	The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.
title_sort	e. coli anti-sigma factor rsd: studies on the specificity and regulation of its expression.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/2f4a584b40fe4fab90b3be6dc478be3a
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The E. coli anti-sigma factor Rsd: studies on the specificity and regulation of its expression.

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