Drosophila MTN: A metazoan copper-thionein related to fungal forms

M. Valls, R. Bofill, N. Romero-Isart, R. Gonzàlez-Duarte, J. Abián, M. Carrascal, P. Gonzàlez-Duarte, M. Capdevila, S. Atrian

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34 Citations (Scopus)


Two Drosophila metallothioneins (MT) have been reported: MTN, a 40 residue peptide including 10 Cys, and MTO, a 43 residue peptide including 12 Cys. However, neither functional nor evolutionary analyses for either of the Drosophila MT are available. Here, heterologous expression of Mtn in Escherichia coli is reported. The metal binding abilities of the Cu- and Zn-MTN complexes conformed in vivo, as well as the features of the Cd- and Cu-aggregates produced by metal replacement in vitro, have been determined by atomic emission spectrometry, circular dichroism and electrospray ionization mass spectrometry. Primary structure relationships with other MT have been examined. The results indicate a close resemblance of MTN to fungal copper-thioneins. Copyright (C) 2000 Federation of European Biochemical Societies.
Original languageEnglish
Pages (from-to)189-194
JournalFEBS Letters
Issue number2-3
Publication statusPublished - 11 Feb 2000


  • Cd(II) binding
  • Cu(I) binding
  • Drosophila metallothionein
  • Molecular evolution
  • Recombinant synthesis
  • Zn(II) binding


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