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dc.contributor.author
Tomas, Mireia
dc.contributor.author
Pagani, María Ayelén
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dc.contributor.author
Andreo, Carlos Santiago
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dc.contributor.author
Capdevila, Mercè
dc.contributor.author
Bofill, Roger
dc.contributor.author
Atrian, Silvia
dc.date.available
2016-10-27T21:19:06Z
dc.date.issued
2014-07
dc.identifier.citation
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
dc.identifier.issn
0949-8257
dc.identifier.uri
http://hdl.handle.net/11336/7841
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Plant Metallothionein
dc.subject
Zinc
dc.subject
Cadmium
dc.subject
Metal-His-Binding
dc.subject
Sulphide Ligands
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
His-containing plant metallothioneins: comparative study of divalent metal-ion binding by plant MT3 and MT4 isoforms
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-03-14T12:49:48Z
dc.journal.volume
19
dc.journal.number
7
dc.journal.pagination
1149-1164
dc.journal.pais
Alemania
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dc.journal.ciudad
Berlin
dc.description.fil
Fil: Tomas, Mireia. Universitat Autonoma de Barcelona; España
dc.description.fil
Fil: Pagani, María Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Capdevila, Mercè. Universitat Autonoma de Barcelona; España
dc.description.fil
Fil: Bofill, Roger. Universitat Autonoma de Barcelona; España
dc.description.fil
Fil: Atrian, Silvia. Universidad de Barcelona; España
dc.journal.title
Journal Of Biological Inorganic Chemistry
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007/s00775-014-1170-1
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00775-014-1170-1
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