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Hierarchical regulation of the NikR-mediated nickel response in Helicobacter pylori

Muller, Cécile ; Bahlawane, Christelle ; Aubert, Sylvie ; Delay, Catherine Marie ; Schauer, Kristine ; Michaud-Soret, Isabelle ; De Reuse, Hilde

Nucleic acids research, 2011-09, Vol.39 (17), p.7564-7575 [Periódico revisado por pares]

England: Oxford University Press

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  • Título:
    Hierarchical regulation of the NikR-mediated nickel response in Helicobacter pylori
  • Autor: Muller, Cécile ; Bahlawane, Christelle ; Aubert, Sylvie ; Delay, Catherine Marie ; Schauer, Kristine ; Michaud-Soret, Isabelle ; De Reuse, Hilde
  • Assuntos: Bacterial Proteins - metabolism ; Biochemistry ; Biochemistry, Molecular Biology ; Gene Expression Regulation, Bacterial - drug effects ; Helicobacter pylori ; Helicobacter pylori - drug effects ; Helicobacter pylori - genetics ; Helicobacter pylori - metabolism ; Kinetics ; Life Sciences ; Molecular Biology ; Nickel - pharmacology ; Repressor Proteins - metabolism ; Transcription, Genetic - drug effects
  • É parte de: Nucleic acids research, 2011-09, Vol.39 (17), p.7564-7575
  • Notas: ObjectType-Article-2
    SourceType-Scholarly Journals-1
    ObjectType-Feature-1
    content type line 23
    PMCID: PMC3177205
    Present addresses: Cécile Muller, USC INRA 2017, Microbiologie de l’Environnement, EA 956, IRBA, Université de Caen, 14032 Caen cedex, France.
    Christelle Bahlawane, Institute for Medical Microbiology and Hospital Epidemiology Hannover Medical School, Carl-Neuberg-Str. 1 D-30625 Hannover, Germany.
    Kristine Schauer, Mécanismes Moléculaires du Transport Intracellulaire, UMR 144 CNRS/Institut Curie, 75248 Paris Cedex 05, France.
  • Descrição: Nickel is an essential metal for Helicobacter pylori, as it is the co-factor of two enzymes crucial for colonization, urease and hydrogenase. Nickel is taken up by specific transporters and its intracellular homeostasis depends on nickel-binding proteins to avoid toxicity. Nickel trafficking is controlled by the Ni(II)-dependent transcriptional regulator NikR. In contrast to other NikR proteins, NikR from H. pylori is a pleiotropic regulator that depending on the target gene acts as an activator or a repressor. We systematically quantified the in vivo Ni2+-NikR response of 11 direct NikR targets that encode functions related to nickel metabolism, four activated and seven repressed genes. Among these, four targets were characterized for the first time (hpn, hpn-like, hydA and hspA) and NikR binding to their promoter regions was demonstrated by electrophoretic mobility shift assays. We found that NikR-dependent repression was generally set up at higher nickel concentrations than activation. Kinetics of the regulation revealed a gradual and temporal NikR-mediated response to nickel where activation of nickel-protection mechanisms takes place before repression of nickel uptake. Our in vivo study demonstrates, for the first time, a chronological hierarchy in the NikR-dependent transcriptional response to nickel that is coherent with the control of nickel homeostasis in H. pylori.
  • Editor: England: Oxford University Press
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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