{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T00:45:33Z","timestamp":1783471533429,"version":"3.55.0"},"reference-count":88,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2022,8,15]],"date-time":"2022-08-15T00:00:00Z","timestamp":1660521600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2022,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Salmonella enterica<\/jats:italic> spp. produce siderophores to bind iron with high affinity and can also use three xenosiderophores secreted by other microorganisms, ferrichrome, coprogen, and ferrioxamine. Here we focused on FoxA, a TonB\u2010dependent transporter of ferrioxamines. Adjacent to <jats:italic>foxA<\/jats:italic> is a gene annotated as a helix\u2010turn\u2010helix (HTH) domain\u2010containing protein, <jats:italic>SL0358<\/jats:italic> (<jats:italic>foxR<\/jats:italic>), in the <jats:italic>Salmonella enterica<\/jats:italic> serovar Typhimurium SL1344 genome. FoxR shares homology with transcriptional regulators belonging to the AraC\/XylS family. <jats:italic>foxR<\/jats:italic> is syntenic with <jats:italic>foxA<\/jats:italic> in the Enterobacteriaceae family, suggesting their functional relatedness. Both <jats:italic>foxA<\/jats:italic> and <jats:italic>foxR<\/jats:italic> are repressed by the ferric uptake regulator (Fur) under iron\u2010rich growth conditions. When iron is scarce, FoxR acts as a transcriptional activator of <jats:italic>foxA<\/jats:italic> by directly binding to its upstream regulatory region. A point mutation in the HTH domain of FoxR abolished this binding, as did mutation of a direct repeat motif in the <jats:italic>foxA<\/jats:italic> upstream regulatory region. Desferrioxamine (DFOE) enhanced FoxR protein stability and <jats:italic>foxA<\/jats:italic> transcription but did not affect the affinity of FoxR binding to the <jats:italic>foxA<\/jats:italic> regulatory region. In summary, we have identified FoxR as a new member of the AraC\/XylS family that regulates xenosiderophore\u2010mediated iron uptake by <jats:italic>S<\/jats:italic>. Typhimurium and likely other Enterobacteriaceae members.<\/jats:p>","DOI":"10.1111\/mmi.14970","type":"journal-article","created":{"date-parts":[[2022,8,4]],"date-time":"2022-08-04T12:30:43Z","timestamp":1659616243000},"page":"369-386","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["<scp>FoxR<\/scp> is an <scp>AraC<\/scp>\u2010like transcriptional regulator of ferrioxamine uptake in <i>Salmonella enterica<\/i>"],"prefix":"10.1111","volume":"118","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2710-2846","authenticated-orcid":false,"given":"Zeus","family":"Salda\u00f1a\u2010Ahuactzi","sequence":"first","affiliation":[{"name":"Paul G. 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