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Int. J. Mol. Sci. 2016, 17(1), 65; doi:10.3390/ijms17010065

Earthworm Lumbricus rubellus MT-2: Metal Binding and Protein Folding of a True Cadmium-MT

1
Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK
2
MRC-PHE Centre for Environment & Health, King´s College London, London SE1 9NH, UK
3
Analytical and Environmental Sciences Division, Faculty of Life Science & Medicine, King’s College London, London SE1 9NH, UK
*
Author to whom correspondence should be addressed.
Academic Editor: Reinhard Dallinger
Received: 30 November 2015 / Revised: 18 December 2015 / Accepted: 24 December 2015 / Published: 5 January 2016
(This article belongs to the Special Issue Metal Metabolism in Animals)
View Full-Text   |   Download PDF [2184 KB, uploaded 5 January 2016]   |  

Abstract

Earthworms express, as most animals, metallothioneins (MTs)—small, cysteine-rich proteins that bind d10 metal ions (Zn(II), Cd(II), or Cu(I)) in clusters. Three MT homologues are known for Lumbricus rubellus, the common red earthworm, one of which, wMT-2, is strongly induced by exposure of worms to cadmium. This study concerns composition, metal binding affinity and metal-dependent protein folding of wMT-2 expressed recombinantly and purified in the presence of Cd(II) and Zn(II). Crucially, whilst a single Cd7wMT-2 species was isolated from wMT-2-expressing E. coli cultures supplemented with Cd(II), expressions in the presence of Zn(II) yielded mixtures. The average affinities of wMT-2 determined for either Cd(II) or Zn(II) are both within normal ranges for MTs; hence, differential behaviour cannot be explained on the basis of overall affinity. Therefore, the protein folding properties of Cd- and Zn-wMT-2 were compared by 1H NMR spectroscopy. This comparison revealed that the protein fold is better defined in the presence of cadmium than in the presence of zinc. These differences in folding and dynamics may be at the root of the differential behaviour of the cadmium- and zinc-bound protein in vitro, and may ultimately also help in distinguishing zinc and cadmium in the earthworm in vivo. View Full-Text
Keywords: metallothionein; cadmium; zinc; selectivity; protein folding; mass spectrometry; NMR spectroscopy metallothionein; cadmium; zinc; selectivity; protein folding; mass spectrometry; NMR spectroscopy
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Kowald, G.R.; Stürzenbaum, S.R.; Blindauer, C.A. Earthworm Lumbricus rubellus MT-2: Metal Binding and Protein Folding of a True Cadmium-MT. Int. J. Mol. Sci. 2016, 17, 65.

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