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Issue 9, 2010
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The isolated Cys2His2 site in EC metallothionein mediates metal-specific protein folding

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Abstract

The selectivity of proteins involved in metal ion homeostasis is an important part of the puzzle to understand how cells allocate the correct metal ions to the correct proteins. Due to their similar ligand-binding properties, and their frequent co-existence in soils, essential zinc and toxic cadmium are a particularly challenging couple. Thus, minimisation of competition of Cd2+ for Zn2+ sites is of crucial importance for organisms that are in direct contact with soil. Amongst these, plants have an especially critical role, due to their importance for nutrition and energy. We have studied an embryo-specific, zinc-binding metallothionein (EC) from wheat by nuclear magnetic resonance, electrospray mass spectrometry, site-directed mutagenesis, and molecular modelling. Wheat EC exploits differences in affinities of Cys4 and Cys2His2 sites for Cd2+ and Zn2+ to achieve metal-selective protein folding. We propose that this may constitute a novel mechanism to discriminate between essential Zn2+ and toxic Cd2+.

Graphical abstract: The isolated Cys2His2 site in EC metallothionein mediates metal-specific protein folding

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Publication details

The article was received on 03 Feb 2010, accepted on 15 Mar 2010 and first published on 30 Mar 2010


Article type: Paper
DOI: 10.1039/C002348E
Mol. BioSyst., 2010,6, 1592-1603

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    The isolated Cys2His2 site in EC metallothionein mediates metal-specific protein folding

    O. I. Leszczyszyn, C. R. J. White and C. A. Blindauer, Mol. BioSyst., 2010, 6, 1592
    DOI: 10.1039/C002348E

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