title: Isolation and characterization of vicH, encoding a new pleiotropic regulator in Vibrio cholerae.
abstract: During the last decade, the hns gene and its product, the H-NS protein, have been extensively studied in Escherichia coli. H-NS-like proteins seem to be widespread in gram-negative bacteria. However, unlike in E. coli and in Salmonella enterica serovar Typhimurium, little is known about their role in the physiology of those organisms. In this report, we describe the isolation of vicH, an hns-like gene in Vibrio cholerae, the etiological agent of cholera. This gene was isolated from a V. cholerae genomic library by complementation of different phenotypes associated with an hns mutation in E. coli. It encodes a 135-amino-acid protein showing approximately 50% identity with both H-NS and StpA in E. coli. Despite a low amino acid conservation in the N-terminal part, VicH is able to cross-react with anti-H-NS antibodies and to form oligomers in vitro. The vicH gene is expressed as a single gene from two promoters in tandem and is induced by cold shock. A V. cholerae wild-type strain expressing a vicHDelta92 gene lacking its 3' end shows pleiotropic alterations with regard to mucoidy and salicin metabolism. Moreover, this strain is unable to swarm on semisolid medium. Similarly, overexpression of the vicH wild-type gene results in an alteration of swarming behavior. This suggests that VicH could be involved in the virulence process in V. cholerae, in particular by affecting flagellum biosynthesis.
authors.affiliation: Unité de Régulation de l'Expression Génétique, Institut Pasteur, F-75724 Paris, France.
authors.forename: C
authors.initials: C
authors.lastname: Tendeng
authors.forename: C
authors.initials: C
authors.lastname: Badaut
authors.forename: E
authors.initials: E
authors.lastname: Krin
authors.forename: P
authors.initials: P
authors.lastname: Gounon
authors.forename: S
authors.initials: S
authors.lastname: Ngo
authors.forename: A
authors.initials: A
authors.lastname: Danchin
authors.forename: S
authors.initials: S
authors.lastname: Rimsky
authors.forename: P
authors.initials: P
authors.lastname: Bertin
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D001483:Base Sequence; D001592:Benzyl Alcohols / Q000378:metabolism; D003001:Cloning, Molecular; D003080:Cold Temperature; D003429:Cross Reactions; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics; D005798:Genes, Bacterial / Q000235:genetics* / Q000502:physiology; D005809:Genes, Regulator; D005816:Genetic Complementation Test; D005960:Glucosides; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D010641:Phenotype; D011135:Polysaccharides, Bacterial / Q000378:metabolism; D011401:Promoter Regions, Genetic / Q000235:genetics; D012329:RNA, Bacterial / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics; D012333:RNA, Messenger / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics; D016415:Sequence Alignment; D014734:Vibrio cholerae / Q000166:cytology / Q000235:genetics* / Q000472:pathogenicity / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D001592:Benzyl Alcohols; D004268:DNA-Binding Proteins; D005960:Glucosides; C031908:H-NS protein, bacteria; D011135:Polysaccharides, Bacterial; D012329:RNA, Bacterial; D012333:RNA, Messenger; C005696:salicin