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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/500
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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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13.13397 |