A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium

Autores
Pescaretti, María de Las Mercedes; Farizano, Juan Vicente; Morero, Roberto Dionisio; Delgado, Monica Alejandra
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The RcsCDB system of Salmonella enterica serovar Typhimurium is implicated in the control of capsule and flagella synthesis. The hybrid sensor RcsC, the phosphotransferase RcsD and the regulator RcsB, constitute the main components of the RcsCDB system. The proposed Rcs signaling cascade involves the autophosphorylation of RcsC and the transfer of the phosphate group to RcsB, mediated by RcsD. We previously reported that the overexpression of rcsB repress the transcription of rcsD by an autoregulation mechanism. Moreover, we demonstrated that during the rcsD repression, the RcsB-dependent flagella modulation remained active. These results suggest that the Rcs phosphorelay mechanism occurs even in the absence of RcsD. In this work, we established the existence of two alternative phosphorelay pathways driving activation of this system. We demonstrated that RcsC and RcsD can act as histidine kinase proteins which, after autophosphorylate, are able to independently transfer the phosphate to RcsB. Our results suggest that these pathways could be activated by different environmental signals, leading different levels of RcsB-phosphorylated to produce a differential gene modulation. These findings contribute to a better understanding of the complexity and importance of the Rcs system activation, where more than one phosphate flow pathway increases the possibilities to exert gene regulation for a quick environmental changes response.
Fil: Pescaretti, María de Las Mercedes. INST.SUP.DE INVEST.BIOLOGICAS;
Fil: Farizano, Juan Vicente. INST.SUP.DE INVEST.BIOLOGICAS;
Fil: Morero, Roberto Dionisio. INST.SUP.DE INVEST.BIOLOGICAS;
Fil: Delgado, Monica Alejandra. INST.SUP.DE INVEST.BIOLOGICAS;
Materia
Salmonella
Rcscdb
Mechanism
Transduction
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:11336/500

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network_name_str CONICET Digital (CONICET)
spelling A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar TyphimuriumPescaretti, María de Las MercedesFarizano, Juan VicenteMorero, Roberto DionisioDelgado, Monica AlejandraSalmonellaRcscdbMechanismTransductionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The RcsCDB system of Salmonella enterica serovar Typhimurium is implicated in the control of capsule and flagella synthesis. The hybrid sensor RcsC, the phosphotransferase RcsD and the regulator RcsB, constitute the main components of the RcsCDB system. The proposed Rcs signaling cascade involves the autophosphorylation of RcsC and the transfer of the phosphate group to RcsB, mediated by RcsD. We previously reported that the overexpression of rcsB repress the transcription of rcsD by an autoregulation mechanism. Moreover, we demonstrated that during the rcsD repression, the RcsB-dependent flagella modulation remained active. These results suggest that the Rcs phosphorelay mechanism occurs even in the absence of RcsD. In this work, we established the existence of two alternative phosphorelay pathways driving activation of this system. We demonstrated that RcsC and RcsD can act as histidine kinase proteins which, after autophosphorylate, are able to independently transfer the phosphate to RcsB. Our results suggest that these pathways could be activated by different environmental signals, leading different levels of RcsB-phosphorylated to produce a differential gene modulation. These findings contribute to a better understanding of the complexity and importance of the Rcs system activation, where more than one phosphate flow pathway increases the possibilities to exert gene regulation for a quick environmental changes response.Fil: Pescaretti, María de Las Mercedes. INST.SUP.DE INVEST.BIOLOGICAS;Fil: Farizano, Juan Vicente. INST.SUP.DE INVEST.BIOLOGICAS;Fil: Morero, Roberto Dionisio. INST.SUP.DE INVEST.BIOLOGICAS;Fil: Delgado, Monica Alejandra. INST.SUP.DE INVEST.BIOLOGICAS;Public Library Science2013-09-04info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/500Pescaretti, María de Las Mercedes; Farizano, Juan Vicente; Morero, Roberto Dionisio; Delgado, Monica Alejandra; A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium; Public Library Science; Plos One; 8; 9; 4-9-2013; 1-101932-6203enginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0072527info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:26Zoai:ri.conicet.gov.ar:11336/500instacron: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:34982025-09-03 10:11:26.472CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
title A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
spellingShingle A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
Pescaretti, María de Las Mercedes
Salmonella
Rcscdb
Mechanism
Transduction
title_short A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
title_full A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
title_fullStr A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
title_full_unstemmed A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
title_sort A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium
dc.creator.none.fl_str_mv Pescaretti, María de Las Mercedes
Farizano, Juan Vicente
Morero, Roberto Dionisio
Delgado, Monica Alejandra
author Pescaretti, María de Las Mercedes
author_facet Pescaretti, María de Las Mercedes
Farizano, Juan Vicente
Morero, Roberto Dionisio
Delgado, Monica Alejandra
author_role author
author2 Farizano, Juan Vicente
Morero, Roberto Dionisio
Delgado, Monica Alejandra
author2_role author
author
author
dc.subject.none.fl_str_mv Salmonella
Rcscdb
Mechanism
Transduction
topic Salmonella
Rcscdb
Mechanism
Transduction
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The RcsCDB system of Salmonella enterica serovar Typhimurium is implicated in the control of capsule and flagella synthesis. The hybrid sensor RcsC, the phosphotransferase RcsD and the regulator RcsB, constitute the main components of the RcsCDB system. The proposed Rcs signaling cascade involves the autophosphorylation of RcsC and the transfer of the phosphate group to RcsB, mediated by RcsD. We previously reported that the overexpression of rcsB repress the transcription of rcsD by an autoregulation mechanism. Moreover, we demonstrated that during the rcsD repression, the RcsB-dependent flagella modulation remained active. These results suggest that the Rcs phosphorelay mechanism occurs even in the absence of RcsD. In this work, we established the existence of two alternative phosphorelay pathways driving activation of this system. We demonstrated that RcsC and RcsD can act as histidine kinase proteins which, after autophosphorylate, are able to independently transfer the phosphate to RcsB. Our results suggest that these pathways could be activated by different environmental signals, leading different levels of RcsB-phosphorylated to produce a differential gene modulation. These findings contribute to a better understanding of the complexity and importance of the Rcs system activation, where more than one phosphate flow pathway increases the possibilities to exert gene regulation for a quick environmental changes response.
Fil: Pescaretti, María de Las Mercedes. INST.SUP.DE INVEST.BIOLOGICAS;
Fil: Farizano, Juan Vicente. INST.SUP.DE INVEST.BIOLOGICAS;
Fil: Morero, Roberto Dionisio. INST.SUP.DE INVEST.BIOLOGICAS;
Fil: Delgado, Monica Alejandra. INST.SUP.DE INVEST.BIOLOGICAS;
description The RcsCDB system of Salmonella enterica serovar Typhimurium is implicated in the control of capsule and flagella synthesis. The hybrid sensor RcsC, the phosphotransferase RcsD and the regulator RcsB, constitute the main components of the RcsCDB system. The proposed Rcs signaling cascade involves the autophosphorylation of RcsC and the transfer of the phosphate group to RcsB, mediated by RcsD. We previously reported that the overexpression of rcsB repress the transcription of rcsD by an autoregulation mechanism. Moreover, we demonstrated that during the rcsD repression, the RcsB-dependent flagella modulation remained active. These results suggest that the Rcs phosphorelay mechanism occurs even in the absence of RcsD. In this work, we established the existence of two alternative phosphorelay pathways driving activation of this system. We demonstrated that RcsC and RcsD can act as histidine kinase proteins which, after autophosphorylate, are able to independently transfer the phosphate to RcsB. Our results suggest that these pathways could be activated by different environmental signals, leading different levels of RcsB-phosphorylated to produce a differential gene modulation. These findings contribute to a better understanding of the complexity and importance of the Rcs system activation, where more than one phosphate flow pathway increases the possibilities to exert gene regulation for a quick environmental changes response.
publishDate 2013
dc.date.none.fl_str_mv 2013-09-04
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
status_str publishedVersion
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/500
Pescaretti, María de Las Mercedes; Farizano, Juan Vicente; Morero, Roberto Dionisio; Delgado, Monica Alejandra; A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium; Public Library Science; Plos One; 8; 9; 4-9-2013; 1-10
1932-6203
url http://hdl.handle.net/11336/500
identifier_str_mv Pescaretti, María de Las Mercedes; Farizano, Juan Vicente; Morero, Roberto Dionisio; Delgado, Monica Alejandra; A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium; Public Library Science; Plos One; 8; 9; 4-9-2013; 1-10
1932-6203
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0072527
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
dc.publisher.none.fl_str_mv Public Library Science
publisher.none.fl_str_mv Public Library 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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