DI-UMONS : Dépôt institutionnel de l’université de Mons

Recherche transversale
(titres de publication, de périodique et noms de colloque inclus)
2013-07-22 - Colloque/Présentation - poster - Anglais - 0 page(s)

Montante Claire , Rubio Magnieto Jenifer , Demeuldre Mélanie , Wattiez Ruddy , "The plasmid-encoded CopB protein in Cupriavidus metallidurans CH34, a key component in the copper resistance?" in International Conference of BioInorganic Chemistry, ICBIC 16, Grenoble, France, 2013

  • Codes CREF : Biochimie (DI3112)
  • Unités de recherche UMONS : Protéomie et Microbiologie (S828)
  • Instituts UMONS : Institut des Biosciences (Biosciences)

Abstract(s) :

(Anglais) Widely spread in the environment, copper is an essential trace element required by all types of cells. This paradoxical micronutrient - both essential and extremely toxic - constrains the microorganisms such as bacteria to develop some resistance mechanisms to tightly control its homeostasis. The ß-proteobacterium Cupriavidus metallidurans stain CH34, an archetype of metallo-resistant bacteria, is able to colonize various industrial sites contaminated with high concentrations of metal ions such as Cu2+, Ni2+, Zn2+, Pb2+, etc. Previous studies have shown that copper resistance in C. metallidurans CH34 would essentially involve the cop cluster on the bacterial pMOL30 plasmid. Even if the function of some Cop proteins is known (e.g. CopA and CopF proteins), most of them are always unknown. The plasmid-encoded CopB protein from C. metallidurans CH34 holds our interest due to the repetition of a methionine-rich motif (10X) MQGMDHSKMQGMDQGS expected to interact with copper and silver. This work focuses on the structure/function relationship of CopB and the specificity of copper/silver interaction with the sequential motif of this protein. We attempt to provide an answer about the fate of copper in the cell by the way of an electron microscopic approach, but also to investigate the localization of the CopB protein in the cell and, to identify its potential protein partners by an immunoprecipitation.