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dc.contributor.author
Palacios, Oscar  
dc.contributor.author
Pagani, María Ayelén  
dc.contributor.author
Perez Rafael, Silvia  
dc.contributor.author
Egg, Margit  
dc.contributor.author
Höckner, Martina  
dc.contributor.author
Brandstätter, Anita  
dc.contributor.author
Capdevila, Merce  
dc.contributor.author
Atrian, Silvia  
dc.contributor.author
Dallinger, Reinhard  
dc.date.available
2017-04-19T18:10:45Z  
dc.date.issued
2011-01  
dc.identifier.citation
Palacios, Oscar; Pagani, María Ayelén; Perez Rafael, Silvia; Egg, Margit; Höckner, Martina; et al.; Shaping mechanisms of metal specificity in a family of metazoan metallothioneins: evolutionary differentiation of mollusc metallothioneins; Biomed Central; Bmc Biology; 9; 4; 1-2011; 1-20  
dc.identifier.issn
1741-7007  
dc.identifier.uri
http://hdl.handle.net/11336/15450  
dc.description.abstract
Background: The degree of metal binding specificity in metalloproteins such as metallothioneins (MTs) can be crucial for their functional accuracy. Unlike most other animal species, pulmonate molluscs possess homometallic MT isoforms loaded with Cu+ or Cd2+. They have, so far, been obtained as native metal-MT complexes from snail tissues, where they are involved in the metabolism of the metal ion species bound to the respective isoform. However, it has not as yet been discerned if their specific metal occupation is the result of a rigid control of metal availability, or isoform expression programming in the hosting tissues or of structural differences of the respective peptides determining the coordinative options for the different metal ions. In this study, the Roman snail (Helix pomatia) Cu-loaded and Cd-loaded isoforms (HpCuMT and HpCdMT) were used as model molecules in order to elucidate the biochemical and evolutionary mechanisms permitting pulmonate MTs to achieve specificity for their cognate metal ion. Results: HpCuMT and HpCdMT were recombinantly synthesized in the presence of Cd2+, Zn2+ or Cu2+ and corresponding metal complexes analysed by electrospray mass spectrometry and circular dichroism (CD) and ultra violet-visible (UV-Vis) spectrophotometry. Both MT isoforms were only able to form unique, homometallic and stable complexes (Cd6-HpCdMT and Cu12-HpCuMT) with their cognate metal ions. Yeast complementation assays demonstrated that the two isoforms assumed metal-specific functions, in agreement with their binding preferences, in heterologous eukaryotic environments. In the snail organism, the functional metal specificity of HpCdMT and HpCuMT was contributed by metal-specific transcription programming and cell-specific expression. Sequence elucidation and phylogenetic analysis of MT isoforms from a number of snail species revealed that they possess an unspecific and two metal-specific MT isoforms, whose metal specificity was achieved exclusively by evolutionary modulation of non-cysteine amino acid positions. Conclusion: The Roman snail HpCdMT and HpCuMT isoforms can thus be regarded as prototypes of isoform families that evolved genuine metal-specificity within pulmonate molluscs. Diversification into these isoforms may have been initiated by gene duplication, followed by speciation and selection towards opposite needs for protecting copper-dominated metabolic pathways from nonessential cadmium. The mechanisms enabling these proteins to be metal-specific could also be relevant for other metalloproteins.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Biomed Central  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Metallothionein  
dc.subject
Helix Pomatia  
dc.subject
Copper  
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Cadmium  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Shaping mechanisms of metal specificity in a family of metazoan metallothioneins: evolutionary differentiation of mollusc metallothioneins  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2017-04-18T14:01:53Z  
dc.journal.volume
9  
dc.journal.number
4  
dc.journal.pagination
1-20  
dc.journal.pais
Reino Unido  
dc.journal.ciudad
Londres  
dc.description.fil
Fil: Palacios, Oscar. Universitat Autonoma de Barcelona; España  
dc.description.fil
Fil: Pagani, María Ayelén. Universidad de Barcelona; España. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina  
dc.description.fil
Fil: Perez Rafael, Silvia. Universitat Autonoma de Barcelona; España  
dc.description.fil
Fil: Egg, Margit. Universidad de Innsbruck; Austria  
dc.description.fil
Fil: Höckner, Martina. Universidad de Innsbruck; Austria  
dc.description.fil
Fil: Brandstätter, Anita. Universidad de Innsbruck; Austria  
dc.description.fil
Fil: Capdevila, Merce. Universitat Autonoma de Barcelona; España  
dc.description.fil
Fil: Atrian, Silvia. Universidad de Barcelona; España  
dc.description.fil
Fil: Dallinger, Reinhard. Universidad de Innsbruck; Austria  
dc.journal.title
Bmc Biology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1186/1741-7007-9-4  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://bmcbiol.biomedcentral.com/articles/10.1186/1741-7007-9-4