Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011
- Autores
- Sobrero, Patricio Martín; Schluter, Jan Phillip; Lanner, Ulrike; Schlosser, Andreas; Becker, Anke; Valverde, Claudio Fabián
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Riboregulation stands for RNA-based control of gene expression. In bacteria, small non-coding RNAs (sRNAs) are a major class of riboregulatory elements, most of which act at the post-transcriptional level by base-pairing target mRNA genes. The RNA chaperone Hfq facilitates antisense interactions between target mRNAs and regulatory sRNAs, thus influencing mRNA stability and/or translation rate. In the α-proteobacterium Sinorhizobium meliloti strain 2011, the identification and detection of multiple sRNAs genes and the broadly pleitropic phenotype associated to the absence of a functional Hfq protein both support the existence of riboregulatory circuits controlling gene expression to ensure the fitness of this bacterium in both free living and symbiotic conditions. In order to identify target mRNAs subject to Hfq-dependent riboregulation, we have compared the proteome of an hfq mutant and the wild type S. meliloti by quantitative proteomics following protein labelling with 15N. Among 2139 univocally identified proteins, a total of 195 proteins showed a differential abundance between the Hfq mutant and the wild type strain; 65 proteins accumulated ≥2-fold whereas 130 were downregulated (≤0.5-fold) in the absence of Hfq. This profound proteomic impact implies a major role for Hfq on regulation of diverse physiological processes in S. meliloti, from transport of small molecules to homeostasis of iron and nitrogen. Changes in the cellular levels of proteins involved in transport of nucleotides, peptides and amino acids, and in iron homeostasis, were confirmed with phenotypic assays. These results represent the first quantitative proteomic analysis in S. meliloti. The comparative analysis of the hfq mutant proteome allowed identification of novel strongly Hfq-regulated genes in S. meliloti.
Fil: Sobrero, Patricio Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Schluter, Jan Phillip. Albert Ludwigs University of Freiburg; Alemania
Fil: Lanner, Ulrike. No especifíca;
Fil: Schlosser, Andreas. No especifíca;
Fil: Becker, Anke. Albert Ludwigs University of Freiburg; Alemania
Fil: Valverde, Claudio Fabián. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina - Materia
-
Hfq
Riboregulation
Sinorhizobium meliloti
Quantitative proteomics - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/197447
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Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011Sobrero, Patricio MartínSchluter, Jan PhillipLanner, UlrikeSchlosser, AndreasBecker, AnkeValverde, Claudio FabiánHfqRiboregulationSinorhizobium melilotiQuantitative proteomicshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Riboregulation stands for RNA-based control of gene expression. In bacteria, small non-coding RNAs (sRNAs) are a major class of riboregulatory elements, most of which act at the post-transcriptional level by base-pairing target mRNA genes. The RNA chaperone Hfq facilitates antisense interactions between target mRNAs and regulatory sRNAs, thus influencing mRNA stability and/or translation rate. In the α-proteobacterium Sinorhizobium meliloti strain 2011, the identification and detection of multiple sRNAs genes and the broadly pleitropic phenotype associated to the absence of a functional Hfq protein both support the existence of riboregulatory circuits controlling gene expression to ensure the fitness of this bacterium in both free living and symbiotic conditions. In order to identify target mRNAs subject to Hfq-dependent riboregulation, we have compared the proteome of an hfq mutant and the wild type S. meliloti by quantitative proteomics following protein labelling with 15N. Among 2139 univocally identified proteins, a total of 195 proteins showed a differential abundance between the Hfq mutant and the wild type strain; 65 proteins accumulated ≥2-fold whereas 130 were downregulated (≤0.5-fold) in the absence of Hfq. This profound proteomic impact implies a major role for Hfq on regulation of diverse physiological processes in S. meliloti, from transport of small molecules to homeostasis of iron and nitrogen. Changes in the cellular levels of proteins involved in transport of nucleotides, peptides and amino acids, and in iron homeostasis, were confirmed with phenotypic assays. These results represent the first quantitative proteomic analysis in S. meliloti. The comparative analysis of the hfq mutant proteome allowed identification of novel strongly Hfq-regulated genes in S. meliloti.Fil: Sobrero, Patricio Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Schluter, Jan Phillip. Albert Ludwigs University of Freiburg; AlemaniaFil: Lanner, Ulrike. No especifíca;Fil: Schlosser, Andreas. No especifíca;Fil: Becker, Anke. Albert Ludwigs University of Freiburg; AlemaniaFil: Valverde, Claudio Fabián. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaPublic Library of Science2012-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/197447Sobrero, Patricio Martín; Schluter, Jan Phillip; Lanner, Ulrike; Schlosser, Andreas; Becker, Anke; et al.; Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011; Public Library of Science; Plos One; 7; 10; 10-2012; 1-111932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://dx.plos.org/10.1371/journal.pone.0048494info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0048494info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:39:33Zoai:ri.conicet.gov.ar:11336/197447instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:39:33.346CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 |
title |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 |
spellingShingle |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 Sobrero, Patricio Martín Hfq Riboregulation Sinorhizobium meliloti Quantitative proteomics |
title_short |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 |
title_full |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 |
title_fullStr |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 |
title_full_unstemmed |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 |
title_sort |
Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011 |
dc.creator.none.fl_str_mv |
Sobrero, Patricio Martín Schluter, Jan Phillip Lanner, Ulrike Schlosser, Andreas Becker, Anke Valverde, Claudio Fabián |
author |
Sobrero, Patricio Martín |
author_facet |
Sobrero, Patricio Martín Schluter, Jan Phillip Lanner, Ulrike Schlosser, Andreas Becker, Anke Valverde, Claudio Fabián |
author_role |
author |
author2 |
Schluter, Jan Phillip Lanner, Ulrike Schlosser, Andreas Becker, Anke Valverde, Claudio Fabián |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Hfq Riboregulation Sinorhizobium meliloti Quantitative proteomics |
topic |
Hfq Riboregulation Sinorhizobium meliloti Quantitative proteomics |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Riboregulation stands for RNA-based control of gene expression. In bacteria, small non-coding RNAs (sRNAs) are a major class of riboregulatory elements, most of which act at the post-transcriptional level by base-pairing target mRNA genes. The RNA chaperone Hfq facilitates antisense interactions between target mRNAs and regulatory sRNAs, thus influencing mRNA stability and/or translation rate. In the α-proteobacterium Sinorhizobium meliloti strain 2011, the identification and detection of multiple sRNAs genes and the broadly pleitropic phenotype associated to the absence of a functional Hfq protein both support the existence of riboregulatory circuits controlling gene expression to ensure the fitness of this bacterium in both free living and symbiotic conditions. In order to identify target mRNAs subject to Hfq-dependent riboregulation, we have compared the proteome of an hfq mutant and the wild type S. meliloti by quantitative proteomics following protein labelling with 15N. Among 2139 univocally identified proteins, a total of 195 proteins showed a differential abundance between the Hfq mutant and the wild type strain; 65 proteins accumulated ≥2-fold whereas 130 were downregulated (≤0.5-fold) in the absence of Hfq. This profound proteomic impact implies a major role for Hfq on regulation of diverse physiological processes in S. meliloti, from transport of small molecules to homeostasis of iron and nitrogen. Changes in the cellular levels of proteins involved in transport of nucleotides, peptides and amino acids, and in iron homeostasis, were confirmed with phenotypic assays. These results represent the first quantitative proteomic analysis in S. meliloti. The comparative analysis of the hfq mutant proteome allowed identification of novel strongly Hfq-regulated genes in S. meliloti. Fil: Sobrero, Patricio Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Schluter, Jan Phillip. Albert Ludwigs University of Freiburg; Alemania Fil: Lanner, Ulrike. No especifíca; Fil: Schlosser, Andreas. No especifíca; Fil: Becker, Anke. Albert Ludwigs University of Freiburg; Alemania Fil: Valverde, Claudio Fabián. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina |
description |
Riboregulation stands for RNA-based control of gene expression. In bacteria, small non-coding RNAs (sRNAs) are a major class of riboregulatory elements, most of which act at the post-transcriptional level by base-pairing target mRNA genes. The RNA chaperone Hfq facilitates antisense interactions between target mRNAs and regulatory sRNAs, thus influencing mRNA stability and/or translation rate. In the α-proteobacterium Sinorhizobium meliloti strain 2011, the identification and detection of multiple sRNAs genes and the broadly pleitropic phenotype associated to the absence of a functional Hfq protein both support the existence of riboregulatory circuits controlling gene expression to ensure the fitness of this bacterium in both free living and symbiotic conditions. In order to identify target mRNAs subject to Hfq-dependent riboregulation, we have compared the proteome of an hfq mutant and the wild type S. meliloti by quantitative proteomics following protein labelling with 15N. Among 2139 univocally identified proteins, a total of 195 proteins showed a differential abundance between the Hfq mutant and the wild type strain; 65 proteins accumulated ≥2-fold whereas 130 were downregulated (≤0.5-fold) in the absence of Hfq. This profound proteomic impact implies a major role for Hfq on regulation of diverse physiological processes in S. meliloti, from transport of small molecules to homeostasis of iron and nitrogen. Changes in the cellular levels of proteins involved in transport of nucleotides, peptides and amino acids, and in iron homeostasis, were confirmed with phenotypic assays. These results represent the first quantitative proteomic analysis in S. meliloti. The comparative analysis of the hfq mutant proteome allowed identification of novel strongly Hfq-regulated genes in S. meliloti. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-10 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/197447 Sobrero, Patricio Martín; Schluter, Jan Phillip; Lanner, Ulrike; Schlosser, Andreas; Becker, Anke; et al.; Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011; Public Library of Science; Plos One; 7; 10; 10-2012; 1-11 1932-6203 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/197447 |
identifier_str_mv |
Sobrero, Patricio Martín; Schluter, Jan Phillip; Lanner, Ulrike; Schlosser, Andreas; Becker, Anke; et al.; Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011; Public Library of Science; Plos One; 7; 10; 10-2012; 1-11 1932-6203 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://dx.plos.org/10.1371/journal.pone.0048494 info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0048494 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Public Library of Science |
publisher.none.fl_str_mv |
Public Library of Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614420967194624 |
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13.070432 |