ArticleInternational journal of molecular sciences2022
The Modular Architecture of Metallothioneins Facilitates Domain Rearrangements and Contributes to Their Evolvability in Metal-Accumulating Mollusks.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- The evolutionary history of chelicerate metallothioneins reveals de novo emergence and metal-binding specialization across the subphylum.Scientific reports · 2026Article
- Myriapod Metallothioneins Conserve the Ancestral Architecture of Arthropods While Displaying Lineage-Specific Adaptations in Metal Binding.Genome biology and evolution · 2026Article
- Experimental recombining of repetitive motifs leads to large functional metallothioneins and demonstrates their modular evolvability potential.Protein science : a publication of the Protein Society · 2025Article
- Metals and metallothionein evolution in snails: a contribution to the concept of metal-specific functionality from an animal model group.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Review
- Differentiated Zn(II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn.Metallomics : integrated biometal science · 2023Article
- Evolution of Cd2+ and Cu+ binding in Helix pomatia metallothioneins.Metallomics : integrated biometal science · 2023Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein domains are independent structural and functional modules that can rearrange to create new proteins. While the evolution of multidomain proteins through the shuffling of different preexisting domains has been well documented, the evolution of domain repeat proteins and the origin of new domains are less understood. Metallothioneins (MTs) provide a good case study considering that they consist of metal-binding domain repeats, some of them with a likely de novo origin. In mollusks, for instance, most MTs are bidomain proteins that arose by lineage-specific rearrangements between six putative domains: α, β1, β2, β3, γ and δ. Some domains have been characterized in bivalves and gastropods, but nothing is known about the MTs and their domains of other Mollusca classes. To fill this gap, we investigated the metal-binding features of NpoMT1 of
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