Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding

Metallothioneins (MTs) are central to metal metabolism and contribute to organismal adaptation to variable metal bioavailability across ecosystems. Although well studied in chordates and mollusks, MTs remain poorly investigated in many arthropod lineages, particularly within the Myriapoda subphylum....

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Autores: Palacios Bonilla, Òscar, Capdevila, Mercè, Albalat Rodríguez, Ricard
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2026
País:España
Institución:Universidad de Oviedo (UNIOVI)
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/227409
Acceso en línea:https://hdl.handle.net/2445/227409
Access Level:acceso abierto
Palabra clave:Artròpodes
Proteïnes
Arthropoda
Proteins
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spelling Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal bindingPalacios Bonilla, ÒscarCapdevila, MercèAlbalat Rodríguez, RicardArtròpodesProteïnesArthropodaProteinsMetallothioneins (MTs) are central to metal metabolism and contribute to organismal adaptation to variable metal bioavailability across ecosystems. Although well studied in chordates and mollusks, MTs remain poorly investigated in many arthropod lineages, particularly within the Myriapoda subphylum. Myriapods, comprising thousands of millipede (Diplopoda) and centipede (Chilopoda) species, are especially relevant for evolutionary studies because they are the sister group to Pancrustacea (crustaceans and insects), and they are some of the earliest arthropods to colonize land. Their MTs therefore provide critical insights into the origin and evolution of arthropod MTs and into the molecular adaptations underlying the colonization of new environments. In this work, we have identified 48 putative MTs from 30 myriapod species, all classified as type 1 (MT1) and occurring in two configurations: the bidomain MT1S (S for short) or the multidomain MT1L (L for long) variants. Evolutionary analyses suggest that MT1S represents the ancestral type not only in myriapods but across Arthropoda, whereas MT1L likely arose during chilopod diversification, probably restricted to the order Glomerida. Despite shared structural features, metal-binding characterization of three myriapod MTs–GminMT1Sa, GminMT1La from <em>Glomeridella minima</em>, and LforMT1S from <em>Lithobius forficatus</em>–revealed marked functional differences. The diplopod proteins GminMT1Sa and GminMT1La displayed a Cd-thionein character, while the chilopod LforMT1S was a multipurpose protein, binding cadmium, zinc, and copper without a clear metal preference. These differences likely reflect distinct metal uptake, retention, and excretion strategies in diplopods and chilopods, associated with their ecological adaptations as peaceful decomposers and voracious predators, respectively.Oxford University Press2026info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/227409Articles publicats en revistes (Genètica, Microbiologia i Estadística)reponame:Dipòsit Digital de la UBinstname:Universidad de Oviedo (UNIOVI)InglésReproducció del document publicat a: https://doi.org/10.1093/gbe/evaf248Genome Biology and Evolution, 2026, vol. 18, num.1, p. 1-24https://doi.org/10.1093/gbe/evaf248cc-by-nc (c) Òscar Palacios et al., 2026http://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/2274092026-05-27T06:46:51Z
dc.title.none.fl_str_mv Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
title Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
spellingShingle Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
Palacios Bonilla, Òscar
Artròpodes
Proteïnes
Arthropoda
Proteins
title_short Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
title_full Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
title_fullStr Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
title_full_unstemmed Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
title_sort Myriapod Metallothioneins conserve the ancestral architecture of Arthropods while displaying lineage-specific adaptations in metal binding
dc.creator.none.fl_str_mv Palacios Bonilla, Òscar
Capdevila, Mercè
Albalat Rodríguez, Ricard
author Palacios Bonilla, Òscar
author_facet Palacios Bonilla, Òscar
Capdevila, Mercè
Albalat Rodríguez, Ricard
author_role author
author2 Capdevila, Mercè
Albalat Rodríguez, Ricard
author2_role author
author
dc.subject.none.fl_str_mv Artròpodes
Proteïnes
Arthropoda
Proteins
topic Artròpodes
Proteïnes
Arthropoda
Proteins
description Metallothioneins (MTs) are central to metal metabolism and contribute to organismal adaptation to variable metal bioavailability across ecosystems. Although well studied in chordates and mollusks, MTs remain poorly investigated in many arthropod lineages, particularly within the Myriapoda subphylum. Myriapods, comprising thousands of millipede (Diplopoda) and centipede (Chilopoda) species, are especially relevant for evolutionary studies because they are the sister group to Pancrustacea (crustaceans and insects), and they are some of the earliest arthropods to colonize land. Their MTs therefore provide critical insights into the origin and evolution of arthropod MTs and into the molecular adaptations underlying the colonization of new environments. In this work, we have identified 48 putative MTs from 30 myriapod species, all classified as type 1 (MT1) and occurring in two configurations: the bidomain MT1S (S for short) or the multidomain MT1L (L for long) variants. Evolutionary analyses suggest that MT1S represents the ancestral type not only in myriapods but across Arthropoda, whereas MT1L likely arose during chilopod diversification, probably restricted to the order Glomerida. Despite shared structural features, metal-binding characterization of three myriapod MTs–GminMT1Sa, GminMT1La from <em>Glomeridella minima</em>, and LforMT1S from <em>Lithobius forficatus</em>–revealed marked functional differences. The diplopod proteins GminMT1Sa and GminMT1La displayed a Cd-thionein character, while the chilopod LforMT1S was a multipurpose protein, binding cadmium, zinc, and copper without a clear metal preference. These differences likely reflect distinct metal uptake, retention, and excretion strategies in diplopods and chilopods, associated with their ecological adaptations as peaceful decomposers and voracious predators, respectively.
publishDate 2026
dc.date.none.fl_str_mv 2026
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/2445/227409
url https://hdl.handle.net/2445/227409
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/10.1093/gbe/evaf248
Genome Biology and Evolution, 2026, vol. 18, num.1, p. 1-24
https://doi.org/10.1093/gbe/evaf248
dc.rights.none.fl_str_mv cc-by-nc (c) Òscar Palacios et al., 2026
http://creativecommons.org/licenses/by-nc/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc (c) Òscar Palacios et al., 2026
http://creativecommons.org/licenses/by-nc/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv Articles publicats en revistes (Genètica, Microbiologia i Estadística)
reponame:Dipòsit Digital de la UB
instname:Universidad de Oviedo (UNIOVI)
instname_str Universidad de Oviedo (UNIOVI)
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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