{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,21]],"date-time":"2025-09-21T18:28:15Z","timestamp":1758479295721,"version":"3.37.3"},"reference-count":40,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2016,5,15]],"date-time":"2016-05-15T00:00:00Z","timestamp":1463270400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Science Foundation of China","doi-asserted-by":"crossref","award":["81428015","81171611"],"award-info":[{"award-number":["81428015","81171611"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Science Foundation of China","doi-asserted-by":"crossref","award":["81201319"],"award-info":[{"award-number":["81201319"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI083640","AI117198"],"award-info":[{"award-number":["AI083640","AI117198"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI119532","AI087678"],"award-info":[{"award-number":["AI119532","AI087678"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2016,5,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            It is well established that the RpoN-RpoS sigma factor (\u03c3\n            <jats:sup>54<\/jats:sup>\n            -\u03c3\n            <jats:sup>S<\/jats:sup>\n            ) cascade plays an essential role in differential gene expression during the enzootic cycle of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Borrelia burgdorferi<\/jats:named-content>\n            , the causative agent of Lyme disease. The RpoN-RpoS pathway is activated by the response regulator\/\u03c3\n            <jats:sup>54<\/jats:sup>\n            -dependent activator (also called bacterial enhancer-binding protein [bEBP]) Rrp2. One unique feature of Rrp2 is that this activator is essential for cell replication, whereas RpoN-RpoS is dispensable for bacterial growth. How Rrp2 controls cell replication, a function that is independent of RpoN-RpoS, remains to be elucidated. In this study, by generating a series of conditional\n            <jats:italic>rrp2<\/jats:italic>\n            mutant strains, we demonstrated that the N-terminal receiver domain of Rrp2 is required for spirochetal growth. Furthermore, a D52A point mutation at the phosphorylation site within the N terminus of Rrp2 abolished cell replication. Mutation of the ATPase motif within the central domain of Rrp2 did not affect spirochetal replication, indicating that phosphorylation-dependent ATPase activity of Rrp2 for \u03c3\n            <jats:sup>54<\/jats:sup>\n            activation is not required for cell growth. However, deletion of the C-terminal domain or a 16-amino-acid truncation of the helix-turn-helix (HTH) DNA-binding motif within the C-terminal domain of Rrp2 abolished spirochetal replication. It was shown that constitutive expression of\n            <jats:italic>rpoS<\/jats:italic>\n            is deleterious to borrelial growth. We showed that the essential nature of Rrp2 is not due to an effect on\n            <jats:italic>rpoS<\/jats:italic>\n            . These data suggest that phosphorylation-dependent oligomerization and DNA binding of Rrp2 likely function as a repressor, independently of the activation of \u03c3\n            <jats:sup>54<\/jats:sup>\n            , controlling an essential step of cell replication in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            .\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Bacterial enhancer-binding proteins (bEBPs) are a unique group of transcriptional activators specifically required for \u03c3\n            <jats:sup>54<\/jats:sup>\n            -dependent gene transcription. This work demonstrates that the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            bEBP, Rrp2, has an additional function that is independent of \u03c3\n            <jats:sup>54<\/jats:sup>\n            , that of its essentiality for spirochetal growth, and such a function is dependent on its N-terminal signal domain and C-terminal DNA-binding domain. These findings expand our knowledge on bEBP and provide a foundation to further study the underlying mechanism of this new function of bEBP.\n          <\/jats:p>","DOI":"10.1128\/jb.01010-15","type":"journal-article","created":{"date-parts":[[2016,3,15]],"date-time":"2016-03-15T02:23:41Z","timestamp":1458008621000},"page":"1543-1552","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":14,"title":["Insight into the Dual Functions of Bacterial Enhancer-Binding Protein Rrp2 of Borrelia burgdorferi"],"prefix":"10.1128","volume":"198","author":[{"given":"Yanping","family":"Yin","sequence":"first","affiliation":[{"name":"Key Laboratory of Laboratory Medicine, Ministry of Education of China, School of Laboratory Medicine, Wenzhou Medical University, Wenzhou, Zhejiang, China"},{"name":"Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Youyun","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xuwu","family":"Xiang","sequence":"additional","affiliation":[{"name":"Key Laboratory of Laboratory Medicine, Ministry of Education of China, School of Laboratory Medicine, Wenzhou Medical University, Wenzhou, Zhejiang, China"},{"name":"Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qian","family":"Wang","sequence":"additional","affiliation":[{"name":"Key Laboratory of Laboratory Medicine, Ministry of Education of China, School of Laboratory Medicine, Wenzhou Medical University, Wenzhou, Zhejiang, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhang-Nv","family":"Yang","sequence":"additional","affiliation":[{"name":"Zhejiang Provincial Center for Disease Control and Prevention, Zhejiang, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jon","family":"Blevins","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yongliang","family":"Lou","sequence":"additional","affiliation":[{"name":"Key Laboratory of Laboratory Medicine, Ministry of Education of China, School of Laboratory Medicine, Wenzhou Medical University, Wenzhou, Zhejiang, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"X. 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