Modularity in Protein Evolution: Modular Organization and De Novo Domain Evolution in Mollusk Metallothioneins. (11th September 2020)

• Record Type: Journal Article
• Authors: Calatayud, Sara; Garcia-Risco, Mario; Pedrini-Martha, Veronika; Eernisse, Douglas J; Dallinger, Reinhard; Palacios, Òscar; Capdevila, Mercè; Albalat, Ricard
• Editors: Satta, Yoko
• Is Part Of: Molecular biology and evolution. Volume 38:Number 2(2021)
• Page Start: 424
• Page End: 436
• Publication Date: 2020-09-11
• Subjects: α -- β1 -- β2 -- β3 -- γ -- δ -- domains -- bi- and multimodular metallothioneins -- cysteine motifs -- de novo evolution -- metal-binding capacity and preference; Molecular biology -- Periodicals; Molecular evolution -- Periodicals; Evolution, Molecular -- Periodicals; Molecular Biology -- Periodicals; 572.8
• DOI: 10.1093/molbev/msaa230
• Languages: English
• ISSNs: 0737-4038

Abstract

Abstract: Metallothioneins (MTs) are proteins devoted to the control of metal homeostasis and detoxification, and therefore, MTs have been crucial for the adaptation of the living beings to variable situations of metal bioavailability. The evolution of MTs is, however, not yet fully understood, and to provide new insights into it, we have investigated the MTs in the diverse classes of Mollusks. We have shown that most molluskan MTs are bimodular proteins that combine six domains—α, β1, β2, β3, γ, and δ—in a lineage-specific manner. We have functionally characterized the Neritimorpha β3 β1 and the Patellogastropoda γβ1 MTs, demonstrating the metal-binding capacity of the new γ domain. Our results have revealed a modular organization of mollusk MT, whose evolution has been impacted by duplication, loss, and de novo emergence of domains. MTs represent a paradigmatic example of modular evolution probably driven by the structural and functional requirements of metal binding.