TY - JOUR
T1 - Drosophila MTN: A metazoan copper-thionein related to fungal forms
AU - Valls, M
AU - Bofill, R
AU - Romero-Isart, N
AU - González-Duarte, R
AU - Abián, Joaquin
AU - Carrascal, M
AU - Gonzàlez-Duarte, P
AU - Capdevila, M
AU - Atrian, Silvia
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. (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. (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
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=uab_pure&SrcAuth=WosAPI&KeyUT=WOS:000085417700012&DestLinkType=FullRecord&DestApp=WOS_CPL
U2 - 10.1016/S0014-5793(00)01149-2
DO - 10.1016/S0014-5793(00)01149-2
M3 - Article
C2 - 10675536
SN - 0014-5793
VL - 467
SP - 189
EP - 194
JO - FEBS Letters
JF - FEBS Letters
IS - 2-3
ER -