{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T03:45:00Z","timestamp":1785815100761,"version":"3.56.0"},"reference-count":57,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2010,3,1]],"date-time":"2010-03-01T00:00:00Z","timestamp":1267401600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2010,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Outer membrane iron receptors are some of the major surface entities that are critical for meningococcal pathogenesis. The gene encoding the meningococcal hemoglobin receptor, HmbR, is both independently transcribed and transcriptionally linked to the upstream gene\n            <jats:italic>hemO<\/jats:italic>\n            , which encodes a heme oxygenase. The MisR\/S two-component system was previously determined to regulate\n            <jats:italic>hmbR<\/jats:italic>\n            transcription, and its\n            <jats:italic>hemO<\/jats:italic>\n            and\n            <jats:italic>hmbR<\/jats:italic>\n            regulatory mechanisms were characterized further here. The expression of\n            <jats:italic>hemO<\/jats:italic>\n            and\n            <jats:italic>hmbR<\/jats:italic>\n            was downregulated in\n            <jats:italic>misR<\/jats:italic>\n            \/\n            <jats:italic>S<\/jats:italic>\n            mutants under both iron-replete and iron-restricted conditions, and the downregulation could be reversed by complementation. No significant changes in expression of other iron receptors were detected, suggesting that the MisR\/S system specifically regulates\n            <jats:italic>hmbR<\/jats:italic>\n            . When hemoglobin was the sole iron source, growth defects were detected in the mutants. Primer extension analysis identified a promoter upstream of the\n            <jats:italic>hemO<\/jats:italic>\n            -associated Correia element (CE) and another promoter at the proximal end of CE, and processed transcripts previously identified for other cotranscribed CEs were also detected, suggesting that there may be posttranscriptional regulation. MisR directly interacts with sequences upstream of the CE and upstream of the\n            <jats:italic>hmbR<\/jats:italic>\n            Fur binding site and thus independently regulates\n            <jats:italic>hemO<\/jats:italic>\n            and\n            <jats:italic>hmbR<\/jats:italic>\n            . Analysis of transcriptional reporters of\n            <jats:italic>hemO<\/jats:italic>\n            and\n            <jats:italic>hmbR<\/jats:italic>\n            further demonstrated the positive role of the MisR\/S system and showed that the transcription of\n            <jats:italic>hmbR<\/jats:italic>\n            initiated from\n            <jats:italic>hemO<\/jats:italic>\n            was significantly reduced. A comparison of the effects of the\n            <jats:italic>misS<\/jats:italic>\n            mutation under iron-replete and iron-depleted conditions suggested that activation by the MisR\/S system and iron-mediated repression by Fur act independently. Thus, the expression of\n            <jats:italic>hemO<\/jats:italic>\n            and\n            <jats:italic>hmbR<\/jats:italic>\n            is coordinately controlled by multiple independent regulatory mechanisms, including the MisR\/S two-component system.\n          <\/jats:p>","DOI":"10.1128\/iai.00363-09","type":"journal-article","created":{"date-parts":[[2009,12,15]],"date-time":"2009-12-15T02:47:48Z","timestamp":1260845268000},"page":"1109-1122","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":15,"title":["Regulatory Role of the MisR\/S Two-Component System in Hemoglobin Utilization in\n            <i>Neisseria meningitidis<\/i>"],"prefix":"10.1128","volume":"78","author":[{"given":"Shuming","family":"Zhao","sequence":"first","affiliation":[{"name":"Department of Medicine, Emory University School of Medicine, Atlanta, Georgia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grisselle E.","family":"Montanez","sequence":"additional","affiliation":[{"name":"Department of Medicine, Emory University School of Medicine, Atlanta, Georgia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pradeep","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Medicine, Emory University School of Medicine, Atlanta, Georgia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Soma","family":"Sannigrahi","sequence":"additional","affiliation":[{"name":"Department of Medicine, Emory University School of Medicine, Atlanta, Georgia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yih-Ling","family":"Tzeng","sequence":"additional","affiliation":[{"name":"Department of Medicine, Emory University School of Medicine, Atlanta, Georgia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(91)90239-U"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1086\/315309"},{"key":"e_1_3_2_4_2","first-page":"163","volume":"18","year":"1995","unstructured":"Angerer, A., S. 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