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The two Caenorhabditis elegans metallothioneins (CeMT-1 and CeMT-2) discriminate between essential zinc and toxic cadmium
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Zeitoun-Ghandour, Sukaina, Charnock, John M., Hodson, Mark E., Leszczyszyn, Oksana I., Blindauer, Claudia A. and Sturzenbaum, Stephen R. (2010) The two Caenorhabditis elegans metallothioneins (CeMT-1 and CeMT-2) discriminate between essential zinc and toxic cadmium. The FEBS Journal, Vol.277 (No.11). pp. 2531-2542. doi:10.1111/j.1742-4658.2010.07667.x
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Official URL: http://dx.doi.org/10.1111/j.1742-4658.2010.07667.x
Abstract
The nematode Caenorhabditis elegans expresses two metallothioneins (MTs), CeMT-1 and CeMT-2, that are believed to be key players in the protection against metal toxicity. In this study, both isoforms were expressed in vitro in the presence of either Zn(II) or Cd(II). Metal binding stoichiometries and affinities were determined by ESI-MS and NMR, respectively. Both isoforms had equal zinc binding ability, but differed in their cadmium binding behaviour, with higher affinity found for CeMT-2. In addition, wild-type C. elegans, single MT knockouts and a double MT knockout allele were exposed to zinc (340 mu m) or cadmium (25 mu m) to investigate effects in vivo. Zinc levels were significantly increased in all knockout strains, but were most pronounced in the CeMT-1 knockout, mtl-1 (tm1770), while cadmium accumulation was highest in the CeMT-2 knockout, mtl-2 (gk125) and the double knockout mtl-1;mtl-2 (zs1). In addition, metal speciation was assessed by X-ray absorption fine-structure spectroscopy. This showed that O-donating, probably phosphate-rich, ligands play a dominant role in maintaining the physiological concentration of zinc, independently of metallothionein status. In contrast, cadmium was shown to coordinate with thiol groups, and the cadmium speciation of the wild-type and the CeMT-2 knockout strain was distinctly different to the CeMT-1 and double knockouts. Taken together, and supported by a simple model calculation, these findings show for the first time that the two MT isoforms have differential affinities towards Cd(II) and Zn(II) at a cellular level, and this is reflected at the protein level. This suggests that the two MT isoforms have distinct in vivo roles.
| Item Type: | Journal Article | ||||
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| Subjects: | Q Science > QD Chemistry Q Science > QL Zoology |
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| Divisions: | Faculty of Science > Chemistry | ||||
| Library of Congress Subject Headings (LCSH): | Chemical affinity, Cadmium, Metallothionein, Zinc, Caenorhabditis elegans, Speciation (Chemistry) | ||||
| Journal or Publication Title: | The FEBS Journal | ||||
| Publisher: | Wiley-Blackwell Publishing Ltd. | ||||
| ISSN: | 1742-464X | ||||
| Official Date: | June 2010 | ||||
| Dates: |
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| Volume: | Vol.277 | ||||
| Number: | No.11 | ||||
| Number of Pages: | 12 | ||||
| Page Range: | pp. 2531-2542 | ||||
| DOI: | 10.1111/j.1742-4658.2010.07667.x | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Royal Society (Great Britain), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Science and Technology Facilities Council (STFC) | ||||
| Grant number: | BB/E025099 (BBSRC), BB/E05099 (STFC) |
Data sourced from Thomson Reuters' Web of Knowledge
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