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Drosophila MTN: a metazoan copper‐thionein related to fungal forms
Author(s) -
Valls M.,
Bofill R.,
Romero-Isart N.,
Gonzàlez-Duarte R.,
Abián J.,
Carrascal M.,
Gonzàlez-Duarte P.,
Capdevila M.,
Atrian S.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01149-2
Subject(s) - circular dichroism , peptide , metalloprotein , copper , chemistry , electrospray ionization , escherichia coli , heterologous expression , mass spectrometry , metal , residue (chemistry) , biochemistry , biophysics , recombinant dna , biology , enzyme , chromatography , organic chemistry , gene
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.