The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.

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 doma...

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Detalles Bibliográficos
Autores: Calatayud, Sara, Garcia-Risco, Mario, Pedrini-Martha, Veronika, Niederwanger, Michael, Dallinger, Reinhard, Palacios Bonilla, Òscar, Capdevila, Mercè, Albalat Rodríguez, Ricard
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/193282
Acceso en línea:https://hdl.handle.net/2445/193282
Access Level:acceso abierto
Palabra clave:Proteïnes
Biologia molecular
Cefalòpodes
Proteins
Molecular biology
Cephalopoda
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spelling The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.Calatayud, SaraGarcia-Risco, MarioPedrini-Martha, VeronikaNiederwanger, MichaelDallinger, ReinhardPalacios Bonilla, ÒscarCapdevila, MercèAlbalat Rodríguez, RicardProteïnesBiologia molecularCefalòpodesProteinsMolecular biologyCephalopodaProtein 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 Nautilus pompilius (Cephalopoda class) and FcaMT1 of Falcidens caudatus (Caudofoveata class). Interestingly, whereas NpoMT1 consists of α and β1 domains and has a prototypical Cd2+ preference, FcaMT1 has a singular preference for Zn2+ ions and a distinct domain composition, including a new Caudofoveata-specific δ domain. Overall, our results suggest that the modular architecture of MTs has contributed to MT evolution during mollusk diversification, and exemplify how modularity increases MT evolvability.MDPI2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/193282Articles publicats en revistes (Genètica, Microbiologia i Estadística)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3390/ijms232415824International Journal of Molecular Sciences, 2022, vol. 23, num. 24, p. 15824https://doi.org/10.3390/ijms232415824cc-by (c) Calatayud, Sara et al., 2022https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1932822026-05-27T06:46:51Z
dc.title.none.fl_str_mv The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
title The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
spellingShingle The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
Calatayud, Sara
Proteïnes
Biologia molecular
Cefalòpodes
Proteins
Molecular biology
Cephalopoda
title_short The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
title_full The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
title_fullStr The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
title_full_unstemmed The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
title_sort The Modular architecture of metallothioneins facilitates domain rearrangements and contributes to their evolvability in metal-accumulating mollusks.
dc.creator.none.fl_str_mv Calatayud, Sara
Garcia-Risco, Mario
Pedrini-Martha, Veronika
Niederwanger, Michael
Dallinger, Reinhard
Palacios Bonilla, Òscar
Capdevila, Mercè
Albalat Rodríguez, Ricard
author Calatayud, Sara
author_facet Calatayud, Sara
Garcia-Risco, Mario
Pedrini-Martha, Veronika
Niederwanger, Michael
Dallinger, Reinhard
Palacios Bonilla, Òscar
Capdevila, Mercè
Albalat Rodríguez, Ricard
author_role author
author2 Garcia-Risco, Mario
Pedrini-Martha, Veronika
Niederwanger, Michael
Dallinger, Reinhard
Palacios Bonilla, Òscar
Capdevila, Mercè
Albalat Rodríguez, Ricard
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Proteïnes
Biologia molecular
Cefalòpodes
Proteins
Molecular biology
Cephalopoda
topic Proteïnes
Biologia molecular
Cefalòpodes
Proteins
Molecular biology
Cephalopoda
description 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 Nautilus pompilius (Cephalopoda class) and FcaMT1 of Falcidens caudatus (Caudofoveata class). Interestingly, whereas NpoMT1 consists of α and β1 domains and has a prototypical Cd2+ preference, FcaMT1 has a singular preference for Zn2+ ions and a distinct domain composition, including a new Caudofoveata-specific δ domain. Overall, our results suggest that the modular architecture of MTs has contributed to MT evolution during mollusk diversification, and exemplify how modularity increases MT evolvability.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/193282
url https://hdl.handle.net/2445/193282
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/ijms232415824
International Journal of Molecular Sciences, 2022, vol. 23, num. 24, p. 15824
https://doi.org/10.3390/ijms232415824
dc.rights.none.fl_str_mv cc-by (c) Calatayud, Sara et al., 2022
https://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Calatayud, Sara et al., 2022
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Genètica, Microbiologia i Estadística)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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