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

被引：33

作者：

Valls, M

Bofill, R

Romero-Isart, N

González-Duarte, R

Abián, J

Carrascal, M

Gonzàlez-Duarte, P

Capdevila, M

Atrian, S

机构：

[1] Univ Barcelona, Fac Biol, Dept Genet, E-08028 Barcelona, Spain

[2] Univ Autonoma Barcelona, Fac Ciencies, Dept Quim Inorgan, E-08193 Barcelona, Spain

[3] CSIC, Inst Invest Biomed Barcelona, Dept Bioanal Med, E-08034 Barcelona, Spain

来源：

FEBS LETTERS | 2000年 / 467卷 / 2-3期

关键词：

Cu(I) binding; Cd(II) binding; Zn(II) binding; molecular evolution; recombinant synthesis; Drosophila metallothionein;

D O I：

10.1016/S0014-5793(00)01149-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2000 Federation of European Biochemical Societies.

引用

页码：189 / 194

页数：6