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dc.contributor.author
Mireia, Tomas
dc.contributor.author
Pagani, María Ayelén
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dc.contributor.author
Andreo, Carlos Santiago
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dc.contributor.author
Capdevila, Merce
dc.contributor.author
Atrian, Silvia
dc.contributor.author
Bofill, Roger
dc.date.available
2024-04-08T11:24:55Z
dc.date.issued
2015-03
dc.identifier.citation
Mireia, Tomas; Pagani, María Ayelén; Andreo, Carlos Santiago; Capdevila, Merce; Atrian, Silvia; et al.; Sunflower metallothionein family characterisation. Study of the Zn(II)- and Cd(II)-binding abilities of the HaMT1 and HaMT2 isoforms; Elsevier Science Inc.; Journal of Inorganic Biochemistry; 148; 3-2015; 35-48
dc.identifier.issn
0162-0134
dc.identifier.uri
http://hdl.handle.net/11336/232263
dc.description.abstract
Plant metallothioneins (MTs) constitute a family of small Cys-rich proteins capable of coordinating metal ions, significantly differing from microbial and animal MTs. They are divided into four subfamilies depending on the Cys pattern in their sequence. In this work, the MT system of the sunflower plant Helianthus annuus) has been defined, with ten genes coding for MTs (HaMT) belonging to the four plant MT subfamilies; three HaMT1, four HaMT2, one HaMT3 and two HaMT4 isoforms. The gene expression pattern and capacity to confer metal resistance to yeast cells have been analysed for at least one member of each subfamily. The divalent metal ion-binding abilities of HaMT1-2 and HaMT2-1 (the isoforms encoded by the most abundantly expressed HaMT1 and HaMT2 isogenes) have been characterised, as HaMT3 and HaMT4 were previously studied. Those isoforms constitute an optimum material to study the effect of Cys number variability on their coordination abilities, as they exhibit additional Cys residues regarding the canonical Cys pattern of each subfamily. Our results show that the variation in the number of Cys does not drastically modify their M(II)-binding abilities, but instead modulates the degree of heterogeneity of the corresponding recombinant syntheses. Significantly, the Zn(II)?HaMT1 complexes were highly susceptible to proteolytic cleavage. The recombinant Cd?MT preparations of both isoforms exhibit significant acid-labile sulphide content-Cd6S8 or Cd7S7 species. Overall results suggest that HaMT2-1 is probably associated with Cd(II) detoxification, in contrast to HaMT1-2, which may be more related to physiological functions, such as metal ion transport and delivery
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc.
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
SUNFLOWER
dc.subject
METALLOTHIONEIN
dc.subject
PLANT MT
dc.subject
Zn-BINDING
dc.subject
Cd-BINDING
dc.subject
BIOLOGICAL FUNCTION
dc.subject.classification
Otros Tópicos Biológicos
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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
Sunflower metallothionein family characterisation. Study of the Zn(II)- and Cd(II)-binding abilities of the HaMT1 and HaMT2 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
2024-04-03T13:36:51Z
dc.identifier.eissn
1873-3344
dc.journal.volume
148
dc.journal.pagination
35-48
dc.journal.pais
Países Bajos
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dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Mireia, Tomas. Universitat Autònoma de Barcelona; España. Universidad de Barcelona; España
dc.description.fil
Fil: Pagani, María Ayelén. 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
dc.description.fil
Fil: Andreo, Carlos Santiago. 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
dc.description.fil
Fil: Capdevila, Merce. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Atrian, Silvia. Universidad de Barcelona; España
dc.description.fil
Fil: Bofill, Roger. Universitat Autònoma de Barcelona; España
dc.journal.title
Journal of Inorganic Biochemistry
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jinorgbio.2015.02.016
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0162013415000598
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