His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms

Autores
Tomas, Mireia; Pagani, María Ayelén; Andreo, Carlos Santiago; Capdevila, Mercè; Bofill, Roger; Atrian, Silvia
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Metallothioneins (MTs) are a superfamily of Cys-rich, low-molecular weight metalloproteins that bind heavy metal ions. These cytosolic metallopeptides, which exist in most living organisms, are thought to be involved in metal homeostasis, metal detoxification, and oxidative stress protection. In this work, we characterise the Zn(II)- and Cd(II)-binding abilities of plant type 3 and type 4 MTs identified in soybean and sunflower, both of them being His-containing peptides. The recombinant metal-MT complexes synthesised in Zn(II) or Cd(II)-enriched Escherichia coli cultures have been analysed by ESI-MS, and CD, ICP-AES, and UV spectroscopies. His-to-Ala type 3 MT mutants have also been constructed and synthesised for the study of the role of His in divalent metal ion coordination. The results show comparable divalent metal-binding capacities for the MTs of type 3, and suggest, for the first time, the participation of their conserved C-term His residues in metal binding. Interesting features for the Zn(II)-binding abilities of type 4 MTs are also reported, as their variable His content may be considered crucial for their biological performance.
Fil: Tomas, Mireia. 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
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Capdevila, Mercè. Universitat Autonoma de Barcelona; España
Fil: Bofill, Roger. Universitat Autonoma de Barcelona; España
Fil: Atrian, Silvia. Universidad de Barcelona; España
Materia
Plant Metallothionein
Zinc
Cadmium
Metal-His-Binding
Sulphide Ligands
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:11336/7841
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/7841
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoformsTomas, MireiaPagani, María AyelénAndreo, Carlos SantiagoCapdevila, MercèBofill, RogerAtrian, SilviaPlant MetallothioneinZincCadmiumMetal-His-BindingSulphide Ligandshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Metallothioneins (MTs) are a superfamily of Cys-rich, low-molecular weight metalloproteins that bind heavy metal ions. These cytosolic metallopeptides, which exist in most living organisms, are thought to be involved in metal homeostasis, metal detoxification, and oxidative stress protection. In this work, we characterise the Zn(II)- and Cd(II)-binding abilities of plant type 3 and type 4 MTs identified in soybean and sunflower, both of them being His-containing peptides. The recombinant metal-MT complexes synthesised in Zn(II) or Cd(II)-enriched Escherichia coli cultures have been analysed by ESI-MS, and CD, ICP-AES, and UV spectroscopies. His-to-Ala type 3 MT mutants have also been constructed and synthesised for the study of the role of His in divalent metal ion coordination. The results show comparable divalent metal-binding capacities for the MTs of type 3, and suggest, for the first time, the participation of their conserved C-term His residues in metal binding. Interesting features for the Zn(II)-binding abilities of type 4 MTs are also reported, as their variable His content may be considered crucial for their biological performance.Fil: Tomas, Mireia. 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); ArgentinaFil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Capdevila, Mercè. Universitat Autonoma de Barcelona; EspañaFil: Bofill, Roger. Universitat Autonoma de Barcelona; EspañaFil: Atrian, Silvia. Universidad de Barcelona; EspañaSpringer2014-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/7841Tomas, Mireia; Pagani, María Ayelén; Andreo, Carlos Santiago; Capdevila, Mercè; Bofill, Roger; et al.; His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms; Springer; Journal Of Biological Inorganic Chemistry; 19; 7; 7-2014; 1149-11640949-8257enginfo:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007/s00775-014-1170-1info:eu-repo/semantics/altIdentifier/doi/10.1007/s00775-014-1170-1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:45:03Zoai:ri.conicet.gov.ar:11336/7841instacron: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:34982025-10-15 15:45:03.317CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
title His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
spellingShingle His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
Tomas, Mireia
Plant Metallothionein
Zinc
Cadmium
Metal-His-Binding
Sulphide Ligands
title_short His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
title_full His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
title_fullStr His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
title_full_unstemmed His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
title_sort His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
dc.creator.none.fl_str_mv Tomas, Mireia
Pagani, María Ayelén
Andreo, Carlos Santiago
Capdevila, Mercè
Bofill, Roger
Atrian, Silvia
author Tomas, Mireia
author_facet Tomas, Mireia
Pagani, María Ayelén
Andreo, Carlos Santiago
Capdevila, Mercè
Bofill, Roger
Atrian, Silvia
author_role author
author2 Pagani, María Ayelén
Andreo, Carlos Santiago
Capdevila, Mercè
Bofill, Roger
Atrian, Silvia
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Plant Metallothionein
Zinc
Cadmium
Metal-His-Binding
Sulphide Ligands
topic Plant Metallothionein
Zinc
Cadmium
Metal-His-Binding
Sulphide Ligands
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 (MTs) are a superfamily of Cys-rich, low-molecular weight metalloproteins that bind heavy metal ions. These cytosolic metallopeptides, which exist in most living organisms, are thought to be involved in metal homeostasis, metal detoxification, and oxidative stress protection. In this work, we characterise the Zn(II)- and Cd(II)-binding abilities of plant type 3 and type 4 MTs identified in soybean and sunflower, both of them being His-containing peptides. The recombinant metal-MT complexes synthesised in Zn(II) or Cd(II)-enriched Escherichia coli cultures have been analysed by ESI-MS, and CD, ICP-AES, and UV spectroscopies. His-to-Ala type 3 MT mutants have also been constructed and synthesised for the study of the role of His in divalent metal ion coordination. The results show comparable divalent metal-binding capacities for the MTs of type 3, and suggest, for the first time, the participation of their conserved C-term His residues in metal binding. Interesting features for the Zn(II)-binding abilities of type 4 MTs are also reported, as their variable His content may be considered crucial for their biological performance.
Fil: Tomas, Mireia. 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
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
Fil: Capdevila, Mercè. Universitat Autonoma de Barcelona; España
Fil: Bofill, Roger. Universitat Autonoma de Barcelona; España
Fil: Atrian, Silvia. Universidad de Barcelona; España
description Metallothioneins (MTs) are a superfamily of Cys-rich, low-molecular weight metalloproteins that bind heavy metal ions. These cytosolic metallopeptides, which exist in most living organisms, are thought to be involved in metal homeostasis, metal detoxification, and oxidative stress protection. In this work, we characterise the Zn(II)- and Cd(II)-binding abilities of plant type 3 and type 4 MTs identified in soybean and sunflower, both of them being His-containing peptides. The recombinant metal-MT complexes synthesised in Zn(II) or Cd(II)-enriched Escherichia coli cultures have been analysed by ESI-MS, and CD, ICP-AES, and UV spectroscopies. His-to-Ala type 3 MT mutants have also been constructed and synthesised for the study of the role of His in divalent metal ion coordination. The results show comparable divalent metal-binding capacities for the MTs of type 3, and suggest, for the first time, the participation of their conserved C-term His residues in metal binding. Interesting features for the Zn(II)-binding abilities of type 4 MTs are also reported, as their variable His content may be considered crucial for their biological performance.
publishDate 2014
dc.date.none.fl_str_mv 2014-07
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/11336/7841
Tomas, Mireia; Pagani, María Ayelén; Andreo, Carlos Santiago; Capdevila, Mercè; Bofill, Roger; et al.; His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms; Springer; Journal Of Biological Inorganic Chemistry; 19; 7; 7-2014; 1149-1164
0949-8257
url http://hdl.handle.net/11336/7841
identifier_str_mv Tomas, Mireia; Pagani, María Ayelén; Andreo, Carlos Santiago; Capdevila, Mercè; Bofill, Roger; et al.; His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms; Springer; Journal Of Biological Inorganic Chemistry; 19; 7; 7-2014; 1149-1164
0949-8257
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007/s00775-014-1170-1
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00775-014-1170-1
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 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
_version_ 1846083551673450496
score 13.22299

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