MTO:: the second member of a Drosophila dual copper-thionein system

被引:30
作者
Domenech, J
Palacios, O
Villarreal, L
González-Duarte, P
Capdevila, M
Atrian, S
机构
[1] Univ Barcelona, Fac Biol, Dept Genet, E-08028 Barcelona, Spain
[2] Univ Autonoma Barcelona, Fac Ciencias, Dept Quim, E-08193 Barcelona, Spain
关键词
Drosophila metallothionein; Cu(I) binding; Cd(II) binding; Zn(II) binding; molecular evolution; recombinant synthesis;
D O I
10.1016/S0014-5793(02)03754-7
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
Drosophila MTO metal binding features were analyzed for comparison with MTN, the paralogous Drosophila metallothionein, and to classify MTO as either zinc- or copper-thionein. This was achieved by a combination of in vivo, in vitro and in silico methodologies. All the results unambiguously classified MTO as a second Drosophila copper-thionein, putting Drosophila forward as the only metazoan in which any zinc-thionein has still to be reported. Interestingly, experimental data only showed minor differences in the coordinative behavior of both MTs, but provided a characteristic spectroscopic fingerprint, revealing the possible binding of chloride anions in certain metal-MTO aggregates. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:72 / 78
页数:7
相关论文
共 35 条
[1]   High resolution solution structure of the protein part of Cu7 metallothionein [J].
Bertini, I ;
Hartmann, HJ ;
Klein, T ;
Liu, GH ;
Luchinat, C ;
Weser, U .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (04) :1008-1018
[2]   Zinc(ll) is required for the in vivo and in vitro folding of mouse copper metallothionein in two domains [J].
Bofill, R ;
Capdevila, M ;
Cols, N ;
Atrian, S ;
Gonzàlez-Duarte, P .
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2001, 6 (04) :405-417
[3]   A new insight into the Ag+ and Cu+ binding sites in the metallothionein β domain [J].
Bofill, R ;
Palacios, O ;
Capdevila, M ;
Cols, N ;
González-Duarte, R ;
Atrian, S ;
González-Duarte, P .
JOURNAL OF INORGANIC BIOCHEMISTRY, 1999, 73 (1-2) :57-64
[4]   Role of a copper-specific metallothionein of the blue crab, Callinectes sapidus, in copper metabolism associated with degradation and synthesis of hemocyanin [J].
Brouwer, M ;
Syring, R ;
Brouwer, TH .
JOURNAL OF INORGANIC BIOCHEMISTRY, 2002, 88 (02) :228-239
[5]   COPPER METALLOTHIONEIN OF YEAST, STRUCTURE OF THE GENE, AND REGULATION OF EXPRESSION [J].
BUTT, TR ;
STERNBERG, EJ ;
GORMAN, JA ;
CLARK, P ;
HAMER, D ;
ROSENBERG, M ;
CROOKE, ST .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (11) :3332-3336
[6]   Recombinant synthesis of mouse Zn3-beta and Zn4-alpha metallothionein 1 domains and characterization of their cadmium(II) binding capacity [J].
Capdevila, M ;
Cols, N ;
RomeroIsart, N ;
GonzalezDuarte, R ;
Atrian, S ;
GonzalezDuarte, P .
CELLULAR AND MOLECULAR LIFE SCIENCES, 1997, 53 (08) :681-688
[7]   In vivo copper- and cadmium-binding ability of mammalian metallothionein β domain [J].
Cols, N ;
Romero-Isart, N ;
Bofill, R ;
Capdevila, M ;
Gonzàlez-Duarte, P ;
Gonzàlez-Duarte, R ;
Atrian, S .
PROTEIN ENGINEERING, 1999, 12 (03) :265-269
[8]  
CULOTTA VC, 1994, J BIOL CHEM, V269, P25295
[9]   Metallothionein in snail Cd and Cu metabolism [J].
Dallinger, R ;
Berger, B ;
Hunziker, P ;
Kagi, JHR .
NATURE, 1997, 388 (6639) :237-238
[10]  
DURLIAT M, 1995, BIOMETALS, V8, P339