{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T17:23:51Z","timestamp":1791048231383,"version":"4.1.0"},"reference-count":49,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2012,5,30]],"date-time":"2012-05-30T00:00:00Z","timestamp":1338336000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2012,7]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p><jats:italic>Brucella<\/jats:italic> spp. are facultative intracellular bacteria pathogenic for many mammalian species including humans, causing a disease called brucellosis. Learning how <jats:italic>Brucella<\/jats:italic> 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. <jats:italic>Brucella<\/jats:italic> 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 <jats:italic>Brucella<\/jats:italic> senses the oxygen tension and triggers its environmental adaptation is unknown. In this work we show that the <jats:italic>Brucella abortus<\/jats:italic> NtrY\/NtrX two\u2010component system is involved in oxygen sensing through a haem group contained in a Per\u2010ARNT\u2010SIM (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 <jats:italic>ntrY<\/jats:italic> 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 <jats:italic>Brucella<\/jats:italic> spp.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2012.08095.x","type":"journal-article","created":{"date-parts":[[2012,5,14]],"date-time":"2012-05-14T22:09:33Z","timestamp":1337033373000},"page":"39-50","source":"Crossref","is-referenced-by-count":78,"title":["The NtrY\/X two\u2010component system of <i>Brucella<\/i> spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes"],"prefix":"10.1111","volume":"85","author":[{"given":"Mariela del Carmen","family":"Carrica","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ignacio","family":"Fernandez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcelo 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