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The structure of these PFs, which are composed of a basal body, a hook, and a filament, is similar to the structure of flagella of other bacteria. To determine if hook formation influences flagellin gene transcription in\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            , we inactivated the hook structural gene\n            <jats:italic>flgE<\/jats:italic>\n            by targeted mutagenesis. In many bacteria, completion of the hook structure serves as a checkpoint for transcriptional control of flagellum synthesis and other chemotaxis and motility genes. Specifically, the hook allows secretion of the anti-sigma factor FlgM and concomitant late gene transcription promoted by \u03c3\n            <jats:sup>28<\/jats:sup>\n            . However, the control of\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            PF synthesis differs from the control of flagellum synthesis in other bacteria; the gene encoding \u03c3\n            <jats:sup>28<\/jats:sup>\n            is not present in the genome of\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            , nor are any \u03c3\n            <jats:sup>28<\/jats:sup>\n            promoter recognition sequences associated with the motility genes. We found that\n            <jats:italic>B. burgdorferi flgE<\/jats:italic>\n            mutants lacked PFs, were rod shaped, and were nonmotile, which substantiates previous evidence that PFs are involved in both cell morphology and motility. Although most motility and chemotaxis gene products accumulated at wild-type levels in the absence of FlgE, mutant cells had markedly decreased levels of the flagellar filament proteins FlaA and FlaB. Further analyses showed that the reduction in the levels of flagellin proteins in the spirochetes lacking FlgE was mediated at the posttranscriptional level. Taken together, our results indicate that in\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            , the completion of the hook does not serve as a checkpoint for transcriptional regulation of flagellum synthesis. In addition, we also present evidence that the hook protein in\n            <jats:italic>B. burgdorferi<\/jats:italic>\n            forms a high-molecular-weight complex and that formation of this complex occurs in the periplasmic space.\n          <\/jats:p>","DOI":"10.1128\/jb.01421-07","type":"journal-article","created":{"date-parts":[[2008,1,12]],"date-time":"2008-01-12T01:46:12Z","timestamp":1200102372000},"page":"1912-1921","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":75,"title":["<i>Borrelia burgdorferi<\/i>\n            Uniquely Regulates Its Motility Genes and Has an Intricate Flagellar Hook-Basal Body Structure"],"prefix":"10.1128","volume":"190","author":[{"given":"Melanie S.","family":"Sal","sequence":"first","affiliation":[{"name":"Department of Microbiology, Immunology, and Cell Biology, Robert C. Byrd Health Sciences Center, West Virginia University, Morgantown, West Virginia 26506-9177"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunhao","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Cell Biology, Robert C. Byrd Health Sciences Center, West Virginia University, Morgantown, West Virginia 26506-9177"},{"name":"Department of Oral Biology, State University of New York at Buffalo, Buffalo, New York 14214"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. A.","family":"Motalab","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Cell Biology, Robert C. 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