ArticleInternational journal of molecular sciences2016
Earthworm Lumbricus rubellus MT-2: Metal Binding and Protein Folding of a True Cadmium-MT.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Review
- Insights into the architecture of earthworm metallothionein genes, powered by long-read genomics and transcriptomics.NAR genomics and bioinformatics · 2026Article
- Metal-Coordination Specificity and Structural Dynamics of C. elegans Metallothionein I: Insights From 3D Modeling and MD Simulations.Proteins · 2026Article
- Article
- Juggling cadmium detoxification and zinc homeostasis: A division of labour between the two C. elegans metallothioneins.Chemosphere · 2024Article
- Cadmium Exchange with Zinc in the Non-Classical Zinc Finger Protein Tristetraprolin.Inorganic chemistry · 2021Article
- Evaluation of gene expression of different molecular biomarkers of stress response as an effect of copper exposure on the earthworm EIsenia Andrei.Ecotoxicology (London, England) · 2019Article
- Further insights into the metal ion binding abilities and the metalation pathway of a plant metallothionein from Musa acuminata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Differential reactivity of closely related zinc(II)-binding metallothioneins from the plant Arabidopsis thaliana.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Modulation of trace element bioavailability for two earthworm species after biochar amendment into a contaminated technosol.Ecotoxicology (London, England) · 2017Article
- Metallothionein from Wild Populations of the African Catfish Clarias gariepinus: From Sequence, Protein Expression and Metal Binding Properties to Transcriptional Biomarker of Metal Pollution.International journal of molecular sciences · 2017Article
- Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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Abstract
Earthworms express, as most animals, metallothioneins (MTs)-small, cysteine-rich proteins that bind d(10) 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.
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