Protein Engineering, Vol. 12, No. 3, 265-269,
March 1999
© 1999 Oxford University Press
In vivo copper- and cadmium-binding ability of mammalian metallothionein ß domain
Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Av. Diagonal 645, 08071-Barcelona, Spain and 1 Departament de Química, Universitat Autònoma de Barcelona, 08193-Bellaterra, Barcelona, Spain
The ß domain of mouse metallothionein 1 (ßMT) was synthesized in Escherichia coli cells grown in the presence of copper or cadmium. Homogenous preparations of Cu–ßMT and Cd–ßMT 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–ßMT structure. The copper-containing ßMT clusters formed inside the cells were very stable. In contrast, the nascent ß peptide, although it showed cadmium binding ability, produced a highly unstable species, whose stoichiometry depended upon culture conditions. The absence of ßMT protein in E.coli protease-proficient hosts grown in cadmium-supplemented medium pointed to drastic proteolysis of a poorly folded ß peptide, somehow enhanced by the presence of cadmium. Possible functional and evolutionary implications of the bioactivity of mammalian ßMT in the presence of monovalent and divalent metal ions are discussed.
Keywords: ß domain/in vivo copper binding/in vivo cadmium binding/metallothionein/recombinant expression
2 To whom correspondence should be addressed
* Made equal contributions to this study
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