Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Barchiesi, Julieta | - |
| dc.creator | Hedin, Nicolas | - |
| dc.creator | Gomez Casati, Diego Fabian | - |
| dc.creator | Ballicora, Miguel | - |
| dc.creator | Busi, María Victoria | - |
| dc.date | 2016-10-28T20:24:42Z | - |
| dc.date | 2016-10-28T20:24:42Z | - |
| dc.date | 2015-10 | - |
| dc.date | 2016-03-14T12:50:52Z | - |
| dc.date.accessioned | 2019-04-29T15:32:32Z | - |
| dc.date.available | 2019-04-29T15:32:32Z | - |
| dc.date.issued | 2016-10-28T20:24:42Z | - |
| dc.date.issued | 2016-10-28T20:24:42Z | - |
| dc.date.issued | 2015-10 | - |
| dc.date.issued | 2016-03-14T12:50:52Z | - |
| dc.identifier | 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 | 1756-0500 | - |
| dc.identifier | http://hdl.handle.net/11336/7854 | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/296116 | - |
| dc.description | 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.description | 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: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina | - |
| dc.description | Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina | - |
| dc.description | Fil: Ballicora, Miguel. Loyola University Chicago; Estados Unidos | - |
| dc.description | Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | BioMed Central | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://bmcresnotes.biomedcentral.com/articles/10.1186/s13104-015-1598-6 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4625611/ | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1186/s13104-015-1598-6 | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.subject | Ostreococcus tauri | - |
| dc.subject | starch | - |
| dc.subject | granule | - |
| dc.subject | starch binding domain | - |
| dc.subject | Bioquímica y Biología Molecular | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | 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:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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