Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model

Autores
Palacios, Oscar; Perez Rafael, Silvia; Pagani, María Ayelén; Dallinger, Reinhard; Atrian, Silvia; Capdevila, Merce
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The Helix pomatia metallothionein (MT) system, namely, its two highly specific forms, HpCdMT and HpCuMT, has offered once again an optimum model to study metal?protein specificity. The present work investigates the most unexplored aspect of the coordination behavior of MT polypeptides with respect to either cognate or noncognate metal ions, as opposed to the standard studies of cognate metal ion coordination. To this end, we analyzed the in vivo synthesis of the corresponding complexes with their noncognate metals, and we performed a detailed spectroscopic and spectrometric study of the Zn2+/Cd2+ and Zn2+/Cu+ in vitro replacement reactions on the initial Zn-HpMT species. An HpCuMTAla site-directed mutant, exhibiting differential Cu+-binding abilities in vivo, was also included in this study. We demonstrate that when an MT binds its cognate metal, it yields well-folded complexes of limited stoichiometry, representative of minimal-energy conformations. In contrast, the incorporation of noncognate metal ions is better attributed to an unspecific reaction of cysteinic thiolate groups with metal ions, which is dependent on their concentration in the surrounding milieu, where no minimal-energy structure is reached, and otherwise, the MT peptide acts as a multidentate ligand that will bind metal ions until its capacity has been saturated. Additionally, we suggest that previous binding of an MT polypeptide with its noncognate metal ion (e.g., binding of Zn2+ to the HpCuMT isoform) may preclude the correct folding of the complex with its cognate metal ion.
Fil: Palacios, Oscar. Universitat Autònoma de Barcelona; España
Fil: Perez Rafael, Silvia. Universitat Autònoma de Barcelona; España
Fil: Pagani, María Ayelén. Universidad de Barcelona; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Dallinger, Reinhard. Universidad de Innsbruck; Austria
Fil: Atrian, Silvia. Universidad de Barcelona; España
Fil: Capdevila, Merce. Universitat Autònoma de Barcelona; España
Materia
HELIX POMATIA
METALLOTHIONEIN
CU-SPECIFIC
CD-SPECIFIC
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/233263
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a modelPalacios, OscarPerez Rafael, SilviaPagani, María AyelénDallinger, ReinhardAtrian, SilviaCapdevila, MerceHELIX POMATIAMETALLOTHIONEINCU-SPECIFICCD-SPECIFIChttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The Helix pomatia metallothionein (MT) system, namely, its two highly specific forms, HpCdMT and HpCuMT, has offered once again an optimum model to study metal?protein specificity. The present work investigates the most unexplored aspect of the coordination behavior of MT polypeptides with respect to either cognate or noncognate metal ions, as opposed to the standard studies of cognate metal ion coordination. To this end, we analyzed the in vivo synthesis of the corresponding complexes with their noncognate metals, and we performed a detailed spectroscopic and spectrometric study of the Zn2+/Cd2+ and Zn2+/Cu+ in vitro replacement reactions on the initial Zn-HpMT species. An HpCuMTAla site-directed mutant, exhibiting differential Cu+-binding abilities in vivo, was also included in this study. We demonstrate that when an MT binds its cognate metal, it yields well-folded complexes of limited stoichiometry, representative of minimal-energy conformations. In contrast, the incorporation of noncognate metal ions is better attributed to an unspecific reaction of cysteinic thiolate groups with metal ions, which is dependent on their concentration in the surrounding milieu, where no minimal-energy structure is reached, and otherwise, the MT peptide acts as a multidentate ligand that will bind metal ions until its capacity has been saturated. Additionally, we suggest that previous binding of an MT polypeptide with its noncognate metal ion (e.g., binding of Zn2+ to the HpCuMT isoform) may preclude the correct folding of the complex with its cognate metal ion.Fil: Palacios, Oscar. Universitat Autònoma de Barcelona; EspañaFil: Perez Rafael, Silvia. Universitat Autònoma de Barcelona; EspañaFil: Pagani, María Ayelén. Universidad de Barcelona; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Dallinger, Reinhard. Universidad de Innsbruck; AustriaFil: Atrian, Silvia. Universidad de Barcelona; EspañaFil: Capdevila, Merce. Universitat Autònoma de Barcelona; EspañaSpringer2014-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/233263Palacios, Oscar; Perez Rafael, Silvia; Pagani, María Ayelén; Dallinger, Reinhard; Atrian, Silvia; et al.; Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model; Springer; Journal of Biological Inorganic Chemistry; 19; 6; 4-2014; 923-9350949-82571432-1327CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s00775-014-1127-4info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00775-014-1127-4info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:04:56Zoai:ri.conicet.gov.ar:11336/233263instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:04:56.786CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
title Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
spellingShingle Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
Palacios, Oscar
HELIX POMATIA
METALLOTHIONEIN
CU-SPECIFIC
CD-SPECIFIC
title_short Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
title_full Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
title_fullStr Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
title_full_unstemmed Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
title_sort Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model
dc.creator.none.fl_str_mv Palacios, Oscar
Perez Rafael, Silvia
Pagani, María Ayelén
Dallinger, Reinhard
Atrian, Silvia
Capdevila, Merce
author Palacios, Oscar
author_facet Palacios, Oscar
Perez Rafael, Silvia
Pagani, María Ayelén
Dallinger, Reinhard
Atrian, Silvia
Capdevila, Merce
author_role author
author2 Perez Rafael, Silvia
Pagani, María Ayelén
Dallinger, Reinhard
Atrian, Silvia
Capdevila, Merce
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv HELIX POMATIA
METALLOTHIONEIN
CU-SPECIFIC
CD-SPECIFIC
topic HELIX POMATIA
METALLOTHIONEIN
CU-SPECIFIC
CD-SPECIFIC
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The Helix pomatia metallothionein (MT) system, namely, its two highly specific forms, HpCdMT and HpCuMT, has offered once again an optimum model to study metal?protein specificity. The present work investigates the most unexplored aspect of the coordination behavior of MT polypeptides with respect to either cognate or noncognate metal ions, as opposed to the standard studies of cognate metal ion coordination. To this end, we analyzed the in vivo synthesis of the corresponding complexes with their noncognate metals, and we performed a detailed spectroscopic and spectrometric study of the Zn2+/Cd2+ and Zn2+/Cu+ in vitro replacement reactions on the initial Zn-HpMT species. An HpCuMTAla site-directed mutant, exhibiting differential Cu+-binding abilities in vivo, was also included in this study. We demonstrate that when an MT binds its cognate metal, it yields well-folded complexes of limited stoichiometry, representative of minimal-energy conformations. In contrast, the incorporation of noncognate metal ions is better attributed to an unspecific reaction of cysteinic thiolate groups with metal ions, which is dependent on their concentration in the surrounding milieu, where no minimal-energy structure is reached, and otherwise, the MT peptide acts as a multidentate ligand that will bind metal ions until its capacity has been saturated. Additionally, we suggest that previous binding of an MT polypeptide with its noncognate metal ion (e.g., binding of Zn2+ to the HpCuMT isoform) may preclude the correct folding of the complex with its cognate metal ion.
Fil: Palacios, Oscar. Universitat Autònoma de Barcelona; España
Fil: Perez Rafael, Silvia. Universitat Autònoma de Barcelona; España
Fil: Pagani, María Ayelén. Universidad de Barcelona; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Dallinger, Reinhard. Universidad de Innsbruck; Austria
Fil: Atrian, Silvia. Universidad de Barcelona; España
Fil: Capdevila, Merce. Universitat Autònoma de Barcelona; España
description The Helix pomatia metallothionein (MT) system, namely, its two highly specific forms, HpCdMT and HpCuMT, has offered once again an optimum model to study metal?protein specificity. The present work investigates the most unexplored aspect of the coordination behavior of MT polypeptides with respect to either cognate or noncognate metal ions, as opposed to the standard studies of cognate metal ion coordination. To this end, we analyzed the in vivo synthesis of the corresponding complexes with their noncognate metals, and we performed a detailed spectroscopic and spectrometric study of the Zn2+/Cd2+ and Zn2+/Cu+ in vitro replacement reactions on the initial Zn-HpMT species. An HpCuMTAla site-directed mutant, exhibiting differential Cu+-binding abilities in vivo, was also included in this study. We demonstrate that when an MT binds its cognate metal, it yields well-folded complexes of limited stoichiometry, representative of minimal-energy conformations. In contrast, the incorporation of noncognate metal ions is better attributed to an unspecific reaction of cysteinic thiolate groups with metal ions, which is dependent on their concentration in the surrounding milieu, where no minimal-energy structure is reached, and otherwise, the MT peptide acts as a multidentate ligand that will bind metal ions until its capacity has been saturated. Additionally, we suggest that previous binding of an MT polypeptide with its noncognate metal ion (e.g., binding of Zn2+ to the HpCuMT isoform) may preclude the correct folding of the complex with its cognate metal ion.
publishDate 2014
dc.date.none.fl_str_mv 2014-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/233263
Palacios, Oscar; Perez Rafael, Silvia; Pagani, María Ayelén; Dallinger, Reinhard; Atrian, Silvia; et al.; Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model; Springer; Journal of Biological Inorganic Chemistry; 19; 6; 4-2014; 923-935
0949-8257
1432-1327
CONICET Digital
CONICET
url http://hdl.handle.net/11336/233263
identifier_str_mv Palacios, Oscar; Perez Rafael, Silvia; Pagani, María Ayelén; Dallinger, Reinhard; Atrian, Silvia; et al.; Cognate and noncognate metal ion coordination in metal-specific metallothioneins: The Helix pomatia system as a model; Springer; Journal of Biological Inorganic Chemistry; 19; 6; 4-2014; 923-935
0949-8257
1432-1327
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s00775-014-1127-4
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00775-014-1127-4
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/vnd.openxmlformats-officedocument.wordprocessingml.document
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dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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