The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes
Brucella spp. are facultative intracellular bacteria pathogenic for many mammalian species including humans, causing a disease called brucellosis. Learning how Brucella adapts to its intracellular niche is crucial for understanding its pathogenesis mechanism, allowing for the development of new and...
Guardado en:
| Autores principales: | , , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0950382X_v85_n1_p39_Carrica |
| Aporte de: |
| id |
todo:paper_0950382X_v85_n1_p39_Carrica |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_0950382X_v85_n1_p39_Carrica2023-10-03T15:50:01Z The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes Carrica, M.C. Fernandez, I. Martí, M.A. Paris, G. Goldbaum, F.A. ferric ion ferrous ion iron nitrate reductase nitric oxide reductase nitrite reductase nitrous oxide reductase oxygen protein histidine kinase protein NtrX protein NtrY unclassified drug animal cell article bacterial gene biosensor Brucella abortus controlled study denitrification enzyme regulation gene expression nonhuman ntrY gene oxidation reduction state oxygen tension priority journal protein domain protein expression regulatory mechanism signal transduction Adaptation, Physiological Animals Brucella abortus Cell Line Denitrification Gene Expression Regulation, Bacterial Heme Mice Nitrogen Operon Oxidation-Reduction Oxygen Phosphorylation Promoter Regions, Genetic Protein Kinases Signal Transduction Brucella Brucella melitensis biovar Abortus Mammalia Brucella spp. are facultative intracellular bacteria pathogenic for many mammalian species including humans, causing a disease called brucellosis. Learning how Brucella adapts to its intracellular niche is crucial for understanding its pathogenesis mechanism, allowing for the development of new and more effective vaccines and treatments against brucellosis. Brucella pathogenesis resides mostly in its ability to adapt to the harsh environmental conditions encountered during host infection such as the oxygen depletion. The mechanism by which Brucella senses the oxygen tension and triggers its environmental adaptation is unknown. In this work we show that the Brucella abortus NtrY/NtrX two-component system is involved in oxygen sensing through a haem group contained in a Per-ARNT-SIM (PAS) domain of the NtrY histidine kinase. The NtrY haem iron can be reduced to the ferrous form and is rapidly oxidized to the ferric form in presence of oxygen. Importantly, we show that the oxidation state of the haem iron modulates the autokinase activity, being the anoxygenic reduced ferrous form the signalling state of NtrY. Also, we show that ntrY gene expression increases under low oxygen tension and that NtrY transfers its signal to its cognate response regulator NtrX, regulating in this way the expression of nitrogen respiration enzymes. Based on these findings, we postulate that NtrY acts as a redox sensor in Brucella spp. © 2012 Blackwell Publishing Ltd. Fil:Martí, M.A. 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_v85_n1_p39_Carrica |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
ferric ion ferrous ion iron nitrate reductase nitric oxide reductase nitrite reductase nitrous oxide reductase oxygen protein histidine kinase protein NtrX protein NtrY unclassified drug animal cell article bacterial gene biosensor Brucella abortus controlled study denitrification enzyme regulation gene expression nonhuman ntrY gene oxidation reduction state oxygen tension priority journal protein domain protein expression regulatory mechanism signal transduction Adaptation, Physiological Animals Brucella abortus Cell Line Denitrification Gene Expression Regulation, Bacterial Heme Mice Nitrogen Operon Oxidation-Reduction Oxygen Phosphorylation Promoter Regions, Genetic Protein Kinases Signal Transduction Brucella Brucella melitensis biovar Abortus Mammalia |
| spellingShingle |
ferric ion ferrous ion iron nitrate reductase nitric oxide reductase nitrite reductase nitrous oxide reductase oxygen protein histidine kinase protein NtrX protein NtrY unclassified drug animal cell article bacterial gene biosensor Brucella abortus controlled study denitrification enzyme regulation gene expression nonhuman ntrY gene oxidation reduction state oxygen tension priority journal protein domain protein expression regulatory mechanism signal transduction Adaptation, Physiological Animals Brucella abortus Cell Line Denitrification Gene Expression Regulation, Bacterial Heme Mice Nitrogen Operon Oxidation-Reduction Oxygen Phosphorylation Promoter Regions, Genetic Protein Kinases Signal Transduction Brucella Brucella melitensis biovar Abortus Mammalia Carrica, M.C. Fernandez, I. Martí, M.A. Paris, G. Goldbaum, F.A. The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes |
| topic_facet |
ferric ion ferrous ion iron nitrate reductase nitric oxide reductase nitrite reductase nitrous oxide reductase oxygen protein histidine kinase protein NtrX protein NtrY unclassified drug animal cell article bacterial gene biosensor Brucella abortus controlled study denitrification enzyme regulation gene expression nonhuman ntrY gene oxidation reduction state oxygen tension priority journal protein domain protein expression regulatory mechanism signal transduction Adaptation, Physiological Animals Brucella abortus Cell Line Denitrification Gene Expression Regulation, Bacterial Heme Mice Nitrogen Operon Oxidation-Reduction Oxygen Phosphorylation Promoter Regions, Genetic Protein Kinases Signal Transduction Brucella Brucella melitensis biovar Abortus Mammalia |
| description |
Brucella spp. are facultative intracellular bacteria pathogenic for many mammalian species including humans, causing a disease called brucellosis. Learning how Brucella adapts to its intracellular niche is crucial for understanding its pathogenesis mechanism, allowing for the development of new and more effective vaccines and treatments against brucellosis. Brucella pathogenesis resides mostly in its ability to adapt to the harsh environmental conditions encountered during host infection such as the oxygen depletion. The mechanism by which Brucella senses the oxygen tension and triggers its environmental adaptation is unknown. In this work we show that the Brucella abortus NtrY/NtrX two-component system is involved in oxygen sensing through a haem group contained in a Per-ARNT-SIM (PAS) domain of the NtrY histidine kinase. The NtrY haem iron can be reduced to the ferrous form and is rapidly oxidized to the ferric form in presence of oxygen. Importantly, we show that the oxidation state of the haem iron modulates the autokinase activity, being the anoxygenic reduced ferrous form the signalling state of NtrY. Also, we show that ntrY gene expression increases under low oxygen tension and that NtrY transfers its signal to its cognate response regulator NtrX, regulating in this way the expression of nitrogen respiration enzymes. Based on these findings, we postulate that NtrY acts as a redox sensor in Brucella spp. © 2012 Blackwell Publishing Ltd. |
| format |
JOUR |
| author |
Carrica, M.C. Fernandez, I. Martí, M.A. Paris, G. Goldbaum, F.A. |
| author_facet |
Carrica, M.C. Fernandez, I. Martí, M.A. Paris, G. Goldbaum, F.A. |
| author_sort |
Carrica, M.C. |
| title |
The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes |
| title_short |
The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes |
| title_full |
The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes |
| title_fullStr |
The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes |
| title_full_unstemmed |
The NtrY/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes |
| title_sort |
ntry/x two-component system of brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes |
| url |
http://hdl.handle.net/20.500.12110/paper_0950382X_v85_n1_p39_Carrica |
| work_keys_str_mv |
AT carricamc thentryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT fernandezi thentryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT martima thentryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT parisg thentryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT goldbaumfa thentryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT carricamc ntryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT fernandezi ntryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT martima ntryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT parisg ntryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes AT goldbaumfa ntryxtwocomponentsystemofbrucellasppactsasaredoxsensorandregulatestheexpressionofnitrogenrespirationenzymes |
| _version_ |
1807317283435970560 |