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Metal-responsive promoter DNA compaction by the ferric uptake regulator.
Roncarati, Davide; Pelliciari, Simone; Doniselli, Nicola; Maggi, Stefano; Vannini, Andrea; Valzania, Luca; Mazzei, Luca; Zambelli, Barbara; Rivetti, Claudio; Danielli, Alberto.
Afiliación
  • Roncarati D; Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, 40126 Bologna, Italy.
  • Pelliciari S; Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, 40126 Bologna, Italy.
  • Doniselli N; Department of Life Sciences, University of Parma, 43124 Parma, Italy.
  • Maggi S; Department of Life Sciences, University of Parma, 43124 Parma, Italy.
  • Vannini A; Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, 40126 Bologna, Italy.
  • Valzania L; Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, 40126 Bologna, Italy.
  • Mazzei L; Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, 40126 Bologna, Italy.
  • Zambelli B; Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, 40126 Bologna, Italy.
  • Rivetti C; Department of Life Sciences, University of Parma, 43124 Parma, Italy.
  • Danielli A; Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, 40126 Bologna, Italy.
Nat Commun ; 7: 12593, 2016 08 25.
Article en En | MEDLINE | ID: mdl-27558202
Short-range DNA looping has been proposed to affect promoter activity in many bacterial species and operator configurations, but only few examples have been experimentally investigated in molecular detail. Here we present evidence for a metal-responsive DNA condensation mechanism controlled by the Helicobacter pylori ferric uptake regulator (Fur), an orthologue of the widespread Fur family of prokaryotic metal-dependent regulators. H. pylori Fur represses the transcription of the essential arsRS acid acclimation operon through iron-responsive oligomerization and DNA compaction, encasing the arsR transcriptional start site in a repressive macromolecular complex. A second metal-dependent regulator NikR functions as nickel-dependent anti-repressor at this promoter, antagonizing the binding of Fur to the operator elements responsible for the DNA condensation. The results allow unifying H. pylori metal ion homeostasis and acid acclimation in a mechanistically coherent model, and demonstrate, for the first time, the existence of a selective metal-responsive DNA compaction mechanism controlling bacterial transcriptional regulation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Represoras / Proteínas Bacterianas / ADN Bacteriano / Helicobacter pylori / Regiones Promotoras Genéticas / Hierro Tipo de estudio: Prognostic_studies Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2016 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Represoras / Proteínas Bacterianas / ADN Bacteriano / Helicobacter pylori / Regiones Promotoras Genéticas / Hierro Tipo de estudio: Prognostic_studies Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2016 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Reino Unido