ArticleFEBS open bio2013
The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
Article in FEBS open bio, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Differentiated Zn(II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn.Metallomics : integrated biometal science · 2023Article
- Tunicates Illuminate the Enigmatic Evolution of Chordate Metallothioneins by Gene Gains and Losses, Independent Modular Expansions, and Functional Convergences.Molecular biology and evolution · 2021Article
- Modular Evolution and Population Variability ofFrontiers in cell and developmental biology · 2021Article
- Interplay between Carbonic Anhydrases and Metallothioneins: Structural Control of Metalation.International journal of molecular sciences · 2020Review
- 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
- Cadmium Protection Strategies--A Hidden Trade-Off?International journal of molecular sciences · 2016Review
- Metallothioneins, unconventional proteins from unconventional animals: a long journey from nematodes to mammals.Biomolecules · 2014Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metallothioneins (MTs) constitute a superfamily of ubiquitous metal-binding proteins of low molecular weight and high Cys content. They are involved in metal homeostasis and detoxification, amongst other proposed biological functions. Two MT isoforms (SpMTA and SpMTB) have been reported in the echinoderm Strongylocentrotus purpuratus (sea urchin), both containing 20 Cys residues and presenting extremely similar sequences, although showing distinct tissular and ontogenic expression patterns. Although exhaustive information is available for the Cd(II)-SpMTA complex, this including the full resolution of its 3D structure, no data has been reported concerning either SpMTA Zn(II) and Cu(I) binding properties, or the characterization of SpMTB at protein level. In this work, both the SpMTA and SpMTB isoforms, as well as their separate α and β domains, have been recombinantly synthesized in the presence of Zn(II), Cd(II) or Cu(II), and the corresponding metal complexes have been analyzed using electrospray mass spectrometry, and CD, ICP-AES and UV-vis spectroscopies. The results clearly show a better performance of isoform A when binding Zn(II) and Cd(II), and of isoform B when coordinating Cu(I). Thus, our results confirm the differential metal binding preference of SpMTA and SpMTB, which, together with the reported induction pattern of the respective genes, highlights how also in Echinodermata the MT polymorphism may be linked to the evolution of different physiological roles.
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