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dc.contributor.author
Barchiesi, Julieta
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Hedin, Nicolas
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Gomez Casati, Diego Fabian
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Ballicora, Miguel
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Busi, María Victoria
dc.date.available
2016-10-28T20:24:42Z
dc.date.issued
2015-10
dc.identifier.citation
Barchiesi, Julieta; Hedin, Nicolas; Gomez Casati, Diego Fabian; Ballicora, Miguel; Busi, María Victoria; Functional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases isoforms; BioMed Central; BMC Research Notes; 8; 1; 10-2015
dc.identifier.issn
1756-0500
dc.identifier.uri
http://hdl.handle.net/11336/7854
dc.description.abstract
Abstract Background: Starch‑binding domains are key modules present in several enzymes involved in polysaccharide metabolism. These non‑catalytic modules have already been described as essential for starch‑binding and the cata‑ lytic activity of starch synthase III from the higher plant Arabidopsis thaliana. In Ostreococcus tauri, a unicellular green alga of the Prasinophyceae family, there are three SSIII isoforms, known as Ostta SSIII‑A, SSIII‑B and SSIII‑C. Results: In this work, using in silico and in vitro characterization techniques, we have demonstrated that Ostta SSIII‑ A, SSIII‑B and SSIII‑C contain two, three and no starch‑binding domains, respectively. Additionally, our phylogenetic analysis has indicated that OsttaSSIII‑B, presenting three N‑terminal SBDs, is the isoform more closely related to higher plant SSIII. Furthermore, the sequence alignment and homology modeling data gathered showed that both the main 3‑D structures of all the modeled domains obtained and the main amino acid residues implicated in starch binding are well conserved in O. tauri SSIII starch‑binding domains. In addition, adsorption assays showed that OsttaSSIII‑A D2 and SSIII‑B D2 domains are the two that make the greatest contribution to amylose and amylopectin binding, while OsttaSSIII‑B D1 is also important for starch binding. Conclusions: The results presented here suggest that differences between OsttaSSIII‑A and SSIII‑B SBDs in the number of and binding of amino acid residues may produce differential affinities for each isoform to polysaccharides. Increasing the knowledge about SBDs may lead to their employment in biomedical and industrial applications. Keywords: Ostreococcus tauri, Starch‑binding domains, Starch synthase, Homology modeling, Adsorption assay
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
Ostreococcus Tauri
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Starch
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Granule
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Starch Binding Domain
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Functional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases 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
2016-03-14T12:50:52Z
dc.journal.volume
8
dc.journal.number
1
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Barchiesi, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.description.fil
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
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Fil: Ballicora, Miguel. Loyola University Chicago; Estados Unidos
dc.description.fil
Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina
dc.journal.title
BMC Research Notes
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://bmcresnotes.biomedcentral.com/articles/10.1186/s13104-015-1598-6
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info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4625611/
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info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1186/s13104-015-1598-6