The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. (Articolo in rivista)

Type
Label
  • The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Ceci P. , Ilari A , Falvo E. , Chiancone E. (2003)
    The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties.
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ceci P. , Ilari A , Falvo E. , Chiancone E. (literal)
Pagina inizio
  • 20319 (literal)
Pagina fine
  • 20326 (literal)
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  • The paper provides new insights into the mechanism of bacterial defence from oxidative damage caused by reactive oxygen species. This goal was reached by cobininng different techniques of molecular biology and biophysics. The experimental data were published in a highly valued scientific journal (impact factor 7,258). The paper has been cited 4 times in international scientific journals. (literal)
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  • 278 (literal)
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  • The paper focusses on the structure-function relationships in Dps (DNA binding protein from starved cells) from Agrobacterium tumefaciens, a Gram-negative bacterium, the causative agent for crown gall tumor disease in dicotyledonous plants. Dps is a key component in the protection of the bacterium from the oxidative damage caused by H2O2 produced by plants during infection. The structural and functional characterization of Dps provides a deeper understanding of the DNA protective action these proteins exert. A. tumefaciens Dps does not bind DNA, in contrast to other members of the family, yet it affords protection due to the ability to bind, oxidize and incorporate iron. This ability suffices to prevent the oxidative damage caused by the hydroxyl radical and thereby provides a molecular explanation for the conservation among all members of the family of the characteristic ferroxidase site, where iron oxidation is carried out. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. (literal)
Abstract
  • Agrobacterium tumefaciens Dps (DNA-binding proteins from starved cells), encoded by the dps gene located on the circular chromosome of this plant pathogen, was cloned, and its structural and functional properties were determined in vitro. In Escherichia coli Dps, the family prototype, the DNA binding properties are thought to be associated with the presence of the lysine-containing N-terminal tail that extends from the protein surface into the solvent. The x-ray crystal structure of A. tumefaciens Dps shows that the positively charged N-terminal tail, which is 11 amino acids shorter than in the E. coli protein, is blocked onto the protein surface. This feature accounts for the lack of interaction with DNA. The intersubunit ferroxidase center characteristic of Dps proteins is conserved and confers to the A. tumefaciens protein a ferritin-like activity that manifests itself in the capacity to oxidize and incorporate iron in the internal cavity and to release it after reduction. In turn, sequestration of Fe(II) correlates with the capacity of A. tumefaciens Dps to reduce the production of hydroxyl radicals from H2O2 through Fenton chemistry. These data demonstrate conclusively that DNA protection from oxidative damage in vitro does not require formation of a Dps-DNA complex. In vivo, the hydroxyl radical scavenging activity of A. tumefaciens Dps may be envisaged to act in concert with catalase A to counteract the toxic effect of H2O2, the major component of the plant defense system when challenged by the bacterium. (literal)
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