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

doi:10.1016/S0014-5793(00)01149-2

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

Department of Chemistry

Research output: Contribution to journal › Article › Research › peer-review

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Abstract

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 language	English
Pages (from-to)	189-194
Journal	FEBS Letters
Volume	467
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(00)01149-2
Publication status	Published - 11 Feb 2000

Keywords

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

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10.1016/S0014-5793(00)01149-2

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title = "Drosophila MTN: A metazoan copper-thionein related to fungal forms",

abstract = "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.",

keywords = "Cd(II) binding, Cu(I) binding, Drosophila metallothionein, Molecular evolution, Recombinant synthesis, Zn(II) binding",

author = "M. Valls and R. Bofill and N. Romero-Isart and R. Gonz{\`a}lez-Duarte and J. Abi{\'a}n and M. Carrascal and P. Gonz{\`a}lez-Duarte and M. Capdevila and S. Atrian",

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doi = "10.1016/S0014-5793(00)01149-2",

language = "English",

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TY - JOUR

T1 - Drosophila MTN: A metazoan copper-thionein related to fungal forms

AU - Valls, M.

AU - Bofill, R.

AU - Romero-Isart, N.

AU - Gonzàlez-Duarte, R.

AU - Abián, J.

AU - Carrascal, M.

AU - Gonzàlez-Duarte, P.

AU - Capdevila, M.

AU - Atrian, S.

PY - 2000/2/11

Y1 - 2000/2/11

N2 - 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.

AB - 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.

KW - Cd(II) binding

KW - Cu(I) binding

KW - Drosophila metallothionein

KW - Molecular evolution

KW - Recombinant synthesis

KW - Zn(II) binding

U2 - 10.1016/S0014-5793(00)01149-2

DO - 10.1016/S0014-5793(00)01149-2

M3 - Article

VL - 467

SP - 189

EP - 194

IS - 2-3

ER -

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

Abstract

Keywords

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