Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation

Abstract The RpoS/σS sigma subunit of RNA polymerase is the master regulator of the general stress response in many Gram-negative bacteria. Extensive studies have been conducted on σS-regulated gene expression at the transcriptional level. In contrast, very limited information regarding the impact o...

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Autores principales:	Magali Lago, Véronique Monteil, Thibaut Douche, Julien Guglielmini, Alexis Criscuolo, Corinne Maufrais, Mariette Matondo, Françoise Norel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/269a55cf5d5b4048bfff1bf7dea0c7b7
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spelling	oai:doaj.org-article:269a55cf5d5b4048bfff1bf7dea0c7b72021-12-02T12:32:44ZProteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation10.1038/s41598-017-02362-32045-2322https://doaj.org/article/269a55cf5d5b4048bfff1bf7dea0c7b72017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02362-3https://doaj.org/toc/2045-2322Abstract The RpoS/σS sigma subunit of RNA polymerase is the master regulator of the general stress response in many Gram-negative bacteria. Extensive studies have been conducted on σS-regulated gene expression at the transcriptional level. In contrast, very limited information regarding the impact of σS on global protein production is available. In this study, we used a mass spectrometry-based proteomics approach to explore the wide σS-dependent proteome of the human pathogen Salmonella enterica serovar Typhimurium. Our present goals were twofold: (1) to survey the protein changes associated with the ΔrpoS mutation and (2) to assess the coding capacity of σS-dependent small RNAs. Our proteomics data, and complementary assays, unravelled the large impact of σS on the Salmonella proteome, and validated expression and σS regulation of twenty uncharacterized small proteins of 27 to 96 amino acids. Furthermore, a large number of genes regulated at the protein level only were identified, suggesting that post-transcriptional regulation is an important component of the σS response. Novel aspects of σS in the control of important catabolic pathways such as myo-inositol, L-fucose, propanediol, and ethanolamine were illuminated by this work, providing new insights into the physiological remodelling involved in bacterial adaptation to a non-actively growing state.Magali LagoVéronique MonteilThibaut DoucheJulien GuglielminiAlexis CriscuoloCorinne MaufraisMariette MatondoFrançoise NorelNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Magali Lago Véronique Monteil Thibaut Douche Julien Guglielmini Alexis Criscuolo Corinne Maufrais Mariette Matondo Françoise Norel Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation
description	Abstract The RpoS/σS sigma subunit of RNA polymerase is the master regulator of the general stress response in many Gram-negative bacteria. Extensive studies have been conducted on σS-regulated gene expression at the transcriptional level. In contrast, very limited information regarding the impact of σS on global protein production is available. In this study, we used a mass spectrometry-based proteomics approach to explore the wide σS-dependent proteome of the human pathogen Salmonella enterica serovar Typhimurium. Our present goals were twofold: (1) to survey the protein changes associated with the ΔrpoS mutation and (2) to assess the coding capacity of σS-dependent small RNAs. Our proteomics data, and complementary assays, unravelled the large impact of σS on the Salmonella proteome, and validated expression and σS regulation of twenty uncharacterized small proteins of 27 to 96 amino acids. Furthermore, a large number of genes regulated at the protein level only were identified, suggesting that post-transcriptional regulation is an important component of the σS response. Novel aspects of σS in the control of important catabolic pathways such as myo-inositol, L-fucose, propanediol, and ethanolamine were illuminated by this work, providing new insights into the physiological remodelling involved in bacterial adaptation to a non-actively growing state.
format	article
author	Magali Lago Véronique Monteil Thibaut Douche Julien Guglielmini Alexis Criscuolo Corinne Maufrais Mariette Matondo Françoise Norel
author_facet	Magali Lago Véronique Monteil Thibaut Douche Julien Guglielmini Alexis Criscuolo Corinne Maufrais Mariette Matondo Françoise Norel
author_sort	Magali Lago
title	Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation
title_short	Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation
title_full	Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation
title_fullStr	Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation
title_full_unstemmed	Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation
title_sort	proteome remodelling by the stress sigma factor rpos/σs in salmonella: identification of small proteins and evidence for post-transcriptional regulation
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/269a55cf5d5b4048bfff1bf7dea0c7b7
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Proteome remodelling by the stress sigma factor RpoS/σS in Salmonella: identification of small proteins and evidence for post-transcriptional regulation

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