tailieunhanh - Báo cáo khoa học: Diversity of metallothioneins in the American oyster, Crassostrea virginica, revealed by transcriptomic and proteomic approaches

Metallothioneins are typically low relative molecular mass (6000–7000), sulfhydryl-rich metal-binding proteins with characteristic repeating cysteine motifs (Cys-X-Cys or Cys-Xn-Cys) and a prolate ellipsoid shape containing single a-andb-domains. While functionally diverse, they play important roles in the homeostasis, detoxification and stress response of metals. The originally reported metallothionein of the American oyster,Crassostrea virginicashowed the canonical molluscanab-domain structure. . | Eur. J. Biochem. 271 1702-1712 2004 FEBS 2004 doi Diversity of metallothioneins in the American oyster Crassostrea virginica revealed by transcriptomic and proteomic approaches Matthew J. Jenny1 Amy H. Ringwood4 Kevin Schey2 Gregory W. Warr3 and Robert W. Chapman4 1Marine Biomedicine and Environmental Sciences Center department of Cell and Molecular Pharmacology and 3Department of Biochemistry and Molecular Biology Medical University of South Carolina Charleston SC USA 4Marine Resources Research Institute South Carolina Department of Natural Resources Charleston SC USA Metallothioneins are typically low relative molecular mass 6000-7000 sulfhydryl-rich metal-binding proteins with characteristic repeating cysteine motifs Cys-X-Cys or Cys-Xn-Cys and a prolate ellipsoid shape containing single a- add b-domains. While functionally diverse they play important roles in the homeostasis detoxification and stress response of metals. The originally reported metallothionein of the American oyster Crassostrea virginica showed the canonical molluscan ab-domain structure. Oyster metallo-thioneins have been characterized as cDNA and as expressed proteins and here it is shown that the previously reported metallothionein is a prototypical member of a subfamily designated as CvMT-I of ab-domain metallothioneins. A second extensive subfamily of oyster metallothioneins designated as CvMT-II has apparently arisen from a a stop mutation that truncates the protein after the a-domain and b a subsequent series of duplication and recombination events that have led to the development of metallothionein isoforms containing one to four a-domains and that lack a b-domain. Analysis of metallothioneins revealed that certain CvMT-I isoforms showed preferential association either with cadmium or with copper and zinc even after exposure to cadmium. These data extend our knowledge of the evolutionary diversification of metallothioneins and indicate differences in .

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