The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.

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 echin...

Descripción completa

Detalles Bibliográficos
Autores: Tomas, Mireia, Domènech Casal, Jordi, Capdevila Vidal, Mercè, Bofill, Roger, Atrian i Ventura, Sílvia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/52244
Acceso en línea:https://hdl.handle.net/2445/52244
Access Level:acceso abierto
Palabra clave:Eriçons de mar
Metal·loproteïnes
Metabolisme
Síntesi proteica
Cadmi
Zinc
Coure
Metalls pesants
Sea urchins
Metalloproteins
Metabolism
Protein synthesis
Cadmium
Copper
Heavy metals
id ES_6ebd5a5a69296a7d3cd75dcee38aa656
oai_identifier_str oai:diposit.ub.edu:2445/52244
network_acronym_str ES
network_name_str España
repository_id_str
spelling The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.Tomas, MireiaDomènech Casal, JordiCapdevila Vidal, MercèBofill, RogerAtrian i Ventura, SílviaEriçons de marMetal·loproteïnesMetabolismeSíntesi proteicaCadmiZincCoureMetalls pesantsSea urchinsMetalloproteinsMetabolismProtein synthesisCadmiumZincCopperHeavy metalsMetallothioneins (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.Elsevier2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/52244Articles publicats en revistes (Genètica, Microbiologia i Estadística)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: http://dx.doi.org/10.1016/j.fob.2013.01.005FEBS Open Bio, 2013, vol. 3, num. , p. 89-100http://dx.doi.org/10.1016/j.fob.2013.01.005cc-by-nc-nd (c) Tomas, M. et al., 2013http://creativecommons.org/licenses/by-nc-nd/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/522442026-05-27T06:46:51Z
dc.title.none.fl_str_mv The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
title The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
spellingShingle The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
Tomas, Mireia
Eriçons de mar
Metal·loproteïnes
Metabolisme
Síntesi proteica
Cadmi
Zinc
Coure
Metalls pesants
Sea urchins
Metalloproteins
Metabolism
Protein synthesis
Cadmium
Zinc
Copper
Heavy metals
title_short The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
title_full The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
title_fullStr The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
title_full_unstemmed The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
title_sort The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences.
dc.creator.none.fl_str_mv Tomas, Mireia
Domènech Casal, Jordi
Capdevila Vidal, Mercè
Bofill, Roger
Atrian i Ventura, Sílvia
author Tomas, Mireia
author_facet Tomas, Mireia
Domènech Casal, Jordi
Capdevila Vidal, Mercè
Bofill, Roger
Atrian i Ventura, Sílvia
author_role author
author2 Domènech Casal, Jordi
Capdevila Vidal, Mercè
Bofill, Roger
Atrian i Ventura, Sílvia
author2_role author
author
author
author
dc.subject.none.fl_str_mv Eriçons de mar
Metal·loproteïnes
Metabolisme
Síntesi proteica
Cadmi
Zinc
Coure
Metalls pesants
Sea urchins
Metalloproteins
Metabolism
Protein synthesis
Cadmium
Zinc
Copper
Heavy metals
topic Eriçons de mar
Metal·loproteïnes
Metabolisme
Síntesi proteica
Cadmi
Zinc
Coure
Metalls pesants
Sea urchins
Metalloproteins
Metabolism
Protein synthesis
Cadmium
Zinc
Copper
Heavy metals
description 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.
publishDate 2013
dc.date.none.fl_str_mv 2013
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/2445/52244
url https://hdl.handle.net/2445/52244
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1016/j.fob.2013.01.005
FEBS Open Bio, 2013, vol. 3, num. , p. 89-100
http://dx.doi.org/10.1016/j.fob.2013.01.005
dc.rights.none.fl_str_mv cc-by-nc-nd (c) Tomas, M. et al., 2013
http://creativecommons.org/licenses/by-nc-nd/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-nd (c) Tomas, M. et al., 2013
http://creativecommons.org/licenses/by-nc-nd/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
_version_ 1869410445533642752
score 15.300724

Similares en LA Referencia