The role of histidine in a copper-specific metallothionein

Autores
Perez Rafael, Silvia; Pagani, María Ayelén; Palacios, Oscar Martín; Dallinger, Reinhard; Capdevila, Merce; Atrian, Silvia
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Metallothioneins achieve metal binding specificity by modulation of their amino acid sequences through evolution. Non-coordinating residues seem to play a key role in this function, and among them histidine may be of particular importance. Here we report how this residue regulates CuI binding to a highly copper specific isoform, the CuMT of the snail Helix pomatia, by analysis of the recombinant complexes yielded by a constructed mutant where this residue has been changed to an alanine.
Fil: Perez Rafael, Silvia. Universitat Autonoma de Barcelona; España
Fil: Pagani, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universitat Autonoma de Barcelona; España
Fil: Palacios, Oscar Martín. Universitat Autonoma de Barcelona; España
Fil: Dallinger, Reinhard. Universidad de Innsbruck; Austria
Fil: Capdevila, Merce. Universitat Autonoma de Barcelona; España
Fil: Atrian, Silvia. Universitat Autonoma de Barcelona; España
Materia
Metallothioneins
Histidine
Cu-Thionein
Helix Pomatia
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:11336/7830
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/7830
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The role of histidine in a copper-specific metallothioneinPerez Rafael, SilviaPagani, María AyelénPalacios, Oscar MartínDallinger, ReinhardCapdevila, MerceAtrian, SilviaMetallothioneinsHistidineCu-ThioneinHelix Pomatiahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Metallothioneins achieve metal binding specificity by modulation of their amino acid sequences through evolution. Non-coordinating residues seem to play a key role in this function, and among them histidine may be of particular importance. Here we report how this residue regulates CuI binding to a highly copper specific isoform, the CuMT of the snail Helix pomatia, by analysis of the recombinant complexes yielded by a constructed mutant where this residue has been changed to an alanine.Fil: Perez Rafael, Silvia. Universitat Autonoma de Barcelona; EspañaFil: Pagani, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universitat Autonoma de Barcelona; EspañaFil: Palacios, Oscar Martín. Universitat Autonoma de Barcelona; EspañaFil: Dallinger, Reinhard. Universidad de Innsbruck; AustriaFil: Capdevila, Merce. Universitat Autonoma de Barcelona; EspañaFil: Atrian, Silvia. Universitat Autonoma de Barcelona; EspañaWiley2013-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/7830Perez Rafael, Silvia; Pagani, María Ayelén; Palacios, Oscar Martín; Dallinger, Reinhard; Capdevila, Merce; et al.; The role of histidine in a copper-specific metallothionein; Wiley; Zeitschrift Fur Anorganische Und Allgemeine Chemie; 639; 8-9; 3-2013; 1356-13600044-2313enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/zaac.201300053/abstractinfo:eu-repo/semantics/altIdentifier/doi/10.1002/zaac.201300053info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:52Zoai:ri.conicet.gov.ar:11336/7830instacron: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:34982025-09-03 10:01:52.258CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The role of histidine in a copper-specific metallothionein
title The role of histidine in a copper-specific metallothionein
spellingShingle The role of histidine in a copper-specific metallothionein
Perez Rafael, Silvia
Metallothioneins
Histidine
Cu-Thionein
Helix Pomatia
title_short The role of histidine in a copper-specific metallothionein
title_full The role of histidine in a copper-specific metallothionein
title_fullStr The role of histidine in a copper-specific metallothionein
title_full_unstemmed The role of histidine in a copper-specific metallothionein
title_sort The role of histidine in a copper-specific metallothionein
dc.creator.none.fl_str_mv Perez Rafael, Silvia
Pagani, María Ayelén
Palacios, Oscar Martín
Dallinger, Reinhard
Capdevila, Merce
Atrian, Silvia
author Perez Rafael, Silvia
author_facet Perez Rafael, Silvia
Pagani, María Ayelén
Palacios, Oscar Martín
Dallinger, Reinhard
Capdevila, Merce
Atrian, Silvia
author_role author
author2 Pagani, María Ayelén
Palacios, Oscar Martín
Dallinger, Reinhard
Capdevila, Merce
Atrian, Silvia
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Metallothioneins
Histidine
Cu-Thionein
Helix Pomatia
topic Metallothioneins
Histidine
Cu-Thionein
Helix Pomatia
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Metallothioneins achieve metal binding specificity by modulation of their amino acid sequences through evolution. Non-coordinating residues seem to play a key role in this function, and among them histidine may be of particular importance. Here we report how this residue regulates CuI binding to a highly copper specific isoform, the CuMT of the snail Helix pomatia, by analysis of the recombinant complexes yielded by a constructed mutant where this residue has been changed to an alanine.
Fil: Perez Rafael, Silvia. Universitat Autonoma de Barcelona; España
Fil: Pagani, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universitat Autonoma de Barcelona; España
Fil: Palacios, Oscar Martín. Universitat Autonoma de Barcelona; España
Fil: Dallinger, Reinhard. Universidad de Innsbruck; Austria
Fil: Capdevila, Merce. Universitat Autonoma de Barcelona; España
Fil: Atrian, Silvia. Universitat Autonoma de Barcelona; España
description Metallothioneins achieve metal binding specificity by modulation of their amino acid sequences through evolution. Non-coordinating residues seem to play a key role in this function, and among them histidine may be of particular importance. Here we report how this residue regulates CuI binding to a highly copper specific isoform, the CuMT of the snail Helix pomatia, by analysis of the recombinant complexes yielded by a constructed mutant where this residue has been changed to an alanine.
publishDate 2013
dc.date.none.fl_str_mv 2013-03
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/11336/7830
Perez Rafael, Silvia; Pagani, María Ayelén; Palacios, Oscar Martín; Dallinger, Reinhard; Capdevila, Merce; et al.; The role of histidine in a copper-specific metallothionein; Wiley; Zeitschrift Fur Anorganische Und Allgemeine Chemie; 639; 8-9; 3-2013; 1356-1360
0044-2313
url http://hdl.handle.net/11336/7830
identifier_str_mv Perez Rafael, Silvia; Pagani, María Ayelén; Palacios, Oscar Martín; Dallinger, Reinhard; Capdevila, Merce; et al.; The role of histidine in a copper-specific metallothionein; Wiley; Zeitschrift Fur Anorganische Und Allgemeine Chemie; 639; 8-9; 3-2013; 1356-1360
0044-2313
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/zaac.201300053/abstract
info:eu-repo/semantics/altIdentifier/doi/10.1002/zaac.201300053
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
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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score 13.13397

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