Drosophila MTN: a metazoan copper-thionein related to fungal forms.

@article{Valls2000DrosophilaMA,
  title={Drosophila MTN: a metazoan copper-thionein related to fungal forms.},
  author={Mar{\'i}a D Valls and Roger Bofill and N{\'u}ria Romero-Isart and Roser Gonz{\`a}lez-Duarte and Joaqu{\'i}n Abi{\'a}n and Montserrat Carrascal and Pilar Gonz{\'a}lez-Duarte and Merc{\`e} Capdevila and Silvia Atrian},
  journal={FEBS letters},
  year={2000},
  volume={467 2-3},
  pages={189-94}
}
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… CONTINUE READING

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