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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/197447

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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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