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Earthworm Lumbricus rubellus MT-2 : metal binding and protein folding of a true Cadmium-MT
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Kowald, Gregory R., Sturzenbaum, Stephen R. and Blindauer, Claudia A. (2016) Earthworm Lumbricus rubellus MT-2 : metal binding and protein folding of a true Cadmium-MT. International Journal of Molecular Sciences, 17 (1). pp. 1-16. 65. doi:10.3390/ijms17010065 ISSN 1422-0067.
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Official URL: http://dx.doi.org/10.3390/ijms17010065
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.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QP Physiology | ||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||||
Library of Congress Subject Headings (LCSH): | Metallothionein, Cadmium, Lumbricus rubellus | ||||||||
Journal or Publication Title: | International Journal of Molecular Sciences | ||||||||
Publisher: | M D P I AG | ||||||||
ISSN: | 1422-0067 | ||||||||
Official Date: | 5 January 2016 | ||||||||
Dates: |
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Volume: | 17 | ||||||||
Number: | 1 | ||||||||
Number of Pages: | 16 | ||||||||
Page Range: | pp. 1-16 | ||||||||
Article Number: | 65 | ||||||||
DOI: | 10.3390/ijms17010065 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||
Date of first compliant deposit: | 28 January 2016 | ||||||||
Date of first compliant Open Access: | 28 January 2016 | ||||||||
Funder: | Engineering and Physical Sciences Research Council (EPSRC), Birmingham Science City, Advantage West Midlands (AWM), European Regional Development Fund (ERDF) |
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