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Expression of HA\/protease requires the alternate sigma factor \u03c3\n            <jats:sup>S<\/jats:sup>\n            (RpoS), encoded by\n            <jats:italic>rpoS<\/jats:italic>\n            . The histone-like nucleoid structuring protein (H-NS) has been shown to repress\n            <jats:italic>rpoS<\/jats:italic>\n            expression in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            . In\n            <jats:italic>V. cholerae<\/jats:italic>\n            strains of the classical biotype, H-NS has been reported to silence virulence gene expression. In this study we examined the role of H-NS in the expression of HA\/protease and motility in an El Tor biotype strain by constructing a \u0394\n            <jats:italic>hns<\/jats:italic>\n            mutant. The \u0394\n            <jats:italic>hns<\/jats:italic>\n            mutant exhibited multiple phenotypes, such as production of cholera toxin in nonpermissive LB medium, reduced resistance to high osmolarity, enhanced resistance to low pH and hydrogen peroxide, and reduced motility. Depletion of H-NS by overexpression of a dominant-negative allele or by deletion of\n            <jats:italic>hns<\/jats:italic>\n            resulted in diminished expression of HA\/protease. Epistasis analysis of HA\/protease expression in \u0394\n            <jats:italic>hns<\/jats:italic>\n            , \u0394\n            <jats:italic>rpoS<\/jats:italic>\n            , and \u0394\n            <jats:italic>hns<\/jats:italic>\n            \u0394\n            <jats:italic>rpoS<\/jats:italic>\n            mutants, analysis of RpoS reporter fusions, quantitative reverse transcription-PCR measurements, and ectopic expression of RpoS in \u0394\n            <jats:italic>rpoS<\/jats:italic>\n            and \u0394\n            <jats:italic>rpoS<\/jats:italic>\n            \u0394\n            <jats:italic>hns<\/jats:italic>\n            mutants showed that H-NS posttranscriptionally enhances RpoS expression. The \u0394\n            <jats:italic>hns<\/jats:italic>\n            mutant exhibited a lower degree of motility and lower levels of expression of\n            <jats:italic>flaA<\/jats:italic>\n            ,\n            <jats:italic>flaC<\/jats:italic>\n            ,\n            <jats:italic>cheR<\/jats:italic>\n            -\n            <jats:italic>2<\/jats:italic>\n            , and\n            <jats:italic>motX<\/jats:italic>\n            mRNAs than the wild type. Comparison of the mRNA abundances of these genes in wild-type, \u0394\n            <jats:italic>hns<\/jats:italic>\n            , \u0394\n            <jats:italic>rpoS<\/jats:italic>\n            , and \u0394\n            <jats:italic>hns<\/jats:italic>\n            \u0394\n            <jats:italic>rpoS<\/jats:italic>\n            strains revealed that deletion of\n            <jats:italic>rpoS<\/jats:italic>\n            had a more severe negative effect on their expression. Interestingly, deletion of\n            <jats:italic>hns<\/jats:italic>\n            in the\n            <jats:italic>rpoS<\/jats:italic>\n            background resulted in higher expression levels of\n            <jats:italic>flaA<\/jats:italic>\n            ,\n            <jats:italic>flaC<\/jats:italic>\n            , and\n            <jats:italic>motX<\/jats:italic>\n            , suggesting that H-NS represses the expression of these genes in the absence of \u03c3\n            <jats:sup>S<\/jats:sup>\n            . Finally, we show that the cyclic AMP receptor protein and H-NS act along the same pathway to positively affect RpoS expression.\n          <\/jats:p>","DOI":"10.1128\/jb.00360-08","type":"journal-article","created":{"date-parts":[[2008,9,13]],"date-time":"2008-09-13T00:44:14Z","timestamp":1221266654000},"page":"7335-7345","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":35,"title":["Role of the Histone-Like Nucleoid Structuring Protein in the Regulation of\n            <i>rpoS<\/i>\n            and RpoS-Dependent Genes in\n            <i>Vibrio cholerae<\/i>"],"prefix":"10.1128","volume":"190","author":[{"given":"Anisia J.","family":"Silva","sequence":"first","affiliation":[{"name":"Department of Microbiology, Biochemistry, and Immunology, Morehouse School of Medicine, 720 Westview Dr., SW, Atlanta, Georgia 30310"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Syed Zafar","family":"Sultan","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Biochemistry, and Immunology, Morehouse School of Medicine, 720 Westview Dr., SW, Atlanta, Georgia 30310"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weili","family":"Liang","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Communicable Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Changping, Beijing 102206, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge A.","family":"Benitez","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Biochemistry, and Immunology, Morehouse School of Medicine, 720 Westview Dr., SW, Atlanta, Georgia 30310"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1046\/j.1365-2958.1997.3151679.x","volume":"24","year":"1997","unstructured":"Atlung, T., and H. 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