Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment
The PhoP/PhoQ two-component system plays an essential role regulating numerous virulence phenotypes in Salmonella enterica. Previous work showed that PhoQ, the sensor protein, switches between the kinase- and the phosphatase-dominant state in response to environmental Mg2+ availability. This switch...
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todo:paper_0950382X_v70_n2_p479_Sciara2023-10-03T15:50:01Z Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment Sciara, M.I. Spagnuolo, C. Jares-Erijman, E. García Véscovi, E. bacterial protein magnesium ion mutant protein PhoP protein protein phoq unclassified drug animal cell article cell vacuole cellular distribution controlled study cytoplasm fluorescence microscopy in vitro study macrophage nonhuman priority journal protein expression protein localization Salmonella enterica transcription initiation Animals Bacterial Proteins Cell Line Cytoplasm Macrophages Magnesium Mice Microscopy, Fluorescence Salmonella enterica Bacteria (microorganisms) Salmonella Salmonella enterica Strawberry crinkle virus The PhoP/PhoQ two-component system plays an essential role regulating numerous virulence phenotypes in Salmonella enterica. Previous work showed that PhoQ, the sensor protein, switches between the kinase- and the phosphatase-dominant state in response to environmental Mg2+ availability. This switch defines the PhoP phosphorylation status and, as a result, the transcriptional activity of this regulator. In this work, using the FlAsH labelling technique, we examine PhoP cytolocalization in response to extracellular Mg2+ limitation in vitro and to the Salmonella-containing vacuole (SCV) environment in macrophage cells. We demonstrate that in these PhoP/PhoQ-inducing environments PhoP displays preferential localization to one cell pole, while being homogeneously distributed in the bacterial cytoplasm in repressing conditions. Polar localization is lost in the absence of PhoQ or when a non-phosphorylatable PhoPD52A mutant is expressed. However, when PhoP transcriptional activation is achieved in a Mg2+- and PhoQ-independent manner, PhoP regains asymmetric polar localization. In addition, we show that, in the analysed conditions, PhoQ cellular distribution does not parallel PhoP location pattern. These findings reveal that PhoP cellular location is dynamic and conditioned by its environmentally defined transcriptional status, showing a new insight in the PhoP/PhoQ system mechanism. © 2008 The Authors. Fil:Spagnuolo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Jares-Erijman, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0950382X_v70_n2_p479_Sciara |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
bacterial protein magnesium ion mutant protein PhoP protein protein phoq unclassified drug animal cell article cell vacuole cellular distribution controlled study cytoplasm fluorescence microscopy in vitro study macrophage nonhuman priority journal protein expression protein localization Salmonella enterica transcription initiation Animals Bacterial Proteins Cell Line Cytoplasm Macrophages Magnesium Mice Microscopy, Fluorescence Salmonella enterica Bacteria (microorganisms) Salmonella Salmonella enterica Strawberry crinkle virus |
| spellingShingle |
bacterial protein magnesium ion mutant protein PhoP protein protein phoq unclassified drug animal cell article cell vacuole cellular distribution controlled study cytoplasm fluorescence microscopy in vitro study macrophage nonhuman priority journal protein expression protein localization Salmonella enterica transcription initiation Animals Bacterial Proteins Cell Line Cytoplasm Macrophages Magnesium Mice Microscopy, Fluorescence Salmonella enterica Bacteria (microorganisms) Salmonella Salmonella enterica Strawberry crinkle virus Sciara, M.I. Spagnuolo, C. Jares-Erijman, E. García Véscovi, E. Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment |
| topic_facet |
bacterial protein magnesium ion mutant protein PhoP protein protein phoq unclassified drug animal cell article cell vacuole cellular distribution controlled study cytoplasm fluorescence microscopy in vitro study macrophage nonhuman priority journal protein expression protein localization Salmonella enterica transcription initiation Animals Bacterial Proteins Cell Line Cytoplasm Macrophages Magnesium Mice Microscopy, Fluorescence Salmonella enterica Bacteria (microorganisms) Salmonella Salmonella enterica Strawberry crinkle virus |
| description |
The PhoP/PhoQ two-component system plays an essential role regulating numerous virulence phenotypes in Salmonella enterica. Previous work showed that PhoQ, the sensor protein, switches between the kinase- and the phosphatase-dominant state in response to environmental Mg2+ availability. This switch defines the PhoP phosphorylation status and, as a result, the transcriptional activity of this regulator. In this work, using the FlAsH labelling technique, we examine PhoP cytolocalization in response to extracellular Mg2+ limitation in vitro and to the Salmonella-containing vacuole (SCV) environment in macrophage cells. We demonstrate that in these PhoP/PhoQ-inducing environments PhoP displays preferential localization to one cell pole, while being homogeneously distributed in the bacterial cytoplasm in repressing conditions. Polar localization is lost in the absence of PhoQ or when a non-phosphorylatable PhoPD52A mutant is expressed. However, when PhoP transcriptional activation is achieved in a Mg2+- and PhoQ-independent manner, PhoP regains asymmetric polar localization. In addition, we show that, in the analysed conditions, PhoQ cellular distribution does not parallel PhoP location pattern. These findings reveal that PhoP cellular location is dynamic and conditioned by its environmentally defined transcriptional status, showing a new insight in the PhoP/PhoQ system mechanism. © 2008 The Authors. |
| format |
JOUR |
| author |
Sciara, M.I. Spagnuolo, C. Jares-Erijman, E. García Véscovi, E. |
| author_facet |
Sciara, M.I. Spagnuolo, C. Jares-Erijman, E. García Véscovi, E. |
| author_sort |
Sciara, M.I. |
| title |
Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment |
| title_short |
Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment |
| title_full |
Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment |
| title_fullStr |
Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment |
| title_full_unstemmed |
Cytolocalization of the PhoP response regulator in Salmonella enterica: Modulation by extracellular Mg2+ and by the SCV environment |
| title_sort |
cytolocalization of the phop response regulator in salmonella enterica: modulation by extracellular mg2+ and by the scv environment |
| url |
http://hdl.handle.net/20.500.12110/paper_0950382X_v70_n2_p479_Sciara |
| work_keys_str_mv |
AT sciarami cytolocalizationofthephopresponseregulatorinsalmonellaentericamodulationbyextracellularmg2andbythescvenvironment AT spagnuoloc cytolocalizationofthephopresponseregulatorinsalmonellaentericamodulationbyextracellularmg2andbythescvenvironment AT jareserijmane cytolocalizationofthephopresponseregulatorinsalmonellaentericamodulationbyextracellularmg2andbythescvenvironment AT garciavescovie cytolocalizationofthephopresponseregulatorinsalmonellaentericamodulationbyextracellularmg2andbythescvenvironment |
| _version_ |
1807323247144861696 |