In vivo copper- and cadmium-binding ability of mammalian metallothionein β domain

Neus Cols, Núria Romero-Isart, Roger Bofill, Mercè Capdevila, Pilar Gonzàlez-Duarte, Roser Gonzàlez-Duarte, Sílvia Atrian

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26 Citations (Scopus)


The β domain of mouse metallothionein 1 (βMT) was synthesized in Escherichia coli cells grown in the presence of copper or cadmium. Homogenous preparations of Cu-βMT and Cd-βMT were used to characterize the corresponding in vivo-conformed metal-clusters, and to compare them with the species obtained in vitro by metal replacement to a canonical Zn3-βMT structure. The copper-containing βMT clusters formed inside the cells were very stable. In contrast, the nascent β peptide, although it showed cadmium binding ability, produced a highly unstable species, whose stoichiometry depended upon culture conditions. The absence of βMT protein in E. coli protease-proficient hosts grown in cadmium-supplemented medium pointed to drastic proteolysis of a poorly folded β peptide, somehow enhanced by the presence of cadmium. Possible functional and evolutionary implications of the bioactivity of mammalian βMT in the presence of monovalent and divalent metal ions are discussed.
Original languageEnglish
Pages (from-to)265-269
JournalProtein Engineering
Issue number3
Publication statusPublished - 15 Apr 1999


  • β domain
  • In vivo cadmium binding
  • In vivo copper binding
  • Metallothionein
  • Recombinant expression


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