title: An ArsR/SmtB family member is involved in the regulation by arsenic of the arsenite oxidase operon in Thiomonas arsenitoxydans.
abstract: The genetic organization of the aioBA operon, encoding the arsenite oxidase of the moderately acidophilic and facultative chemoautotrophic bacterium Thiomonas arsenitoxydans, is different from that of the aioBA operon in the other arsenite oxidizers, in that it encodes AioF, a metalloprotein belonging to the ArsR/SmtB family. AioF is stabilized by arsenite, arsenate, or antimonite but not molybdate. Arsenic is tightly attached to AioF, likely by cysteine residues. When loaded with arsenite or arsenate, AioF is able to bind specifically to the regulatory region of the aio operon at two distinct positions. In Thiomonas arsenitoxydans, the promoters of aioX and aioB are convergent, suggesting that transcriptional interference occurs. These results indicate that the regulation of the aioBA operon is more complex in Thiomonas arsenitoxydans than in the other aioBA containing arsenite oxidizers and that the arsenic binding protein AioF is involved in this regulation. On the basis of these data, a model to explain the tight control of aioBA expression by arsenic in Thiomonas arsenitoxydans is proposed.
authors.affiliation: Aix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France.
authors.forename: Danielle
authors.initials: D
authors.lastname: Moinier
authors.affiliation: Aix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France.
authors.forename: Djamila
authors.initials: D
authors.lastname: Slyemi
authors.affiliation: Aix-Marseille Université, CNRS, Plateforme Protéine Production et Criblage FR3479, Marseille, France.
authors.forename: Deborah
authors.initials: D
authors.lastname: Byrne
authors.affiliation: Aix-Marseille Université, CNRS, Plateforme Protéomique FR3479, Marseille, France.
authors.forename: Sabrina
authors.initials: S
authors.lastname: Lignon
authors.affiliation: Aix-Marseille Université, CNRS, Plateforme Protéomique FR3479, Marseille, France.
authors.forename: Régine
authors.initials: R
authors.lastname: Lebrun
authors.affiliation: Aix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France.
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Talla
authors.affiliation: Aix-Marseille Université, CNRS, Laboratoire de Chimie Bactérienne UMR7283, Marseille, France bonnefoy@imm.cnrs.fr.
authors.forename: Violaine
authors.initials: V
authors.lastname: Bonnefoy
mesh_terms: D000595:Amino Acid Sequence; D000965:Antimony / Q000494:pharmacology; D001149:Arsenates / Q000494:pharmacology; D001151:Arsenic / Q000737:chemistry / Q000494:pharmacology*; D018053:Arsenites / Q000494:pharmacology; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D020562:Betaproteobacteria / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism*; D001665:Binding Sites; D003545:Cysteine / Q000737:chemistry; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D008969:Molecular Sequence Data; D008982:Molybdenum / Q000494:pharmacology; D009876:Operon; D010088:Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D001149:Arsenates; D018053:Arsenites; D001426:Bacterial Proteins; D011994:Recombinant Proteins; C061374:antimonite; D008982:Molybdenum; D000965:Antimony; D010088:Oxidoreductases; C078179:arsenite oxidase; D003545:Cysteine; D001151:Arsenic
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