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DNA secondary structure formation by DNA shuffling of the conserved domains of the Cry protein of Bacillus thuringiensis

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dc.contributor.authorPinzón Reyes, Efraín-Hernandospa
dc.contributor.authorSierra, Daniel A.spa
dc.contributor.authorSuárez Barrera, Miguel Orlandospa
dc.contributor.authorOrduz, Sergiospa
dc.contributor.authorFlorez, Alvaro M.spa
dc.date.accessioned2019-06-26T13:11:52Zspa
dc.date.available2019-06-26T13:11:52Zspa
dc.date.issued2017-12spa
dc.description10 p.spa
dc.description.abstractBackground The Cry toxins, or δ-endotoxins, are a diverse group of proteins produced by Bacillus thuringiensis. While DNA secondary structures are biologically relevant, it is unknown if such structures are formed in regions encoding conserved domains of Cry toxins under shuffling conditions. We analyzed 5 holotypes that encode Cry toxins and that grouped into 4 clusters according to their phylogenetic closeness. The mean number of DNA secondary structures that formed and the mean Gibbs free energy (ΔG¯¯¯¯¯¯¯¯) were determined by an in silico analysis using different experimental DNA shuffling scenarios. In terms of spontaneity, shuffling efficiency was directly proportional to the formation of secondary structures but inversely proportional to ∆G. Results The results showed a shared thermodynamic pattern for each cluster and relationships among sequences that are phylogenetically close at the protein level. The regions of the cry11Aa, Ba and Bb genes that encode domain I showed more spontaneity and thus a greater tendency to form secondary structures (<∆G). In the region of domain III; this tendency was lower (>∆G) in the cry11Ba and Bb genes. Proteins that are phylogenetically closer to Cry11Ba and Cry11Bb, such as Cry2Aa and Cry18Aa, maintained the same thermodynamic pattern. More distant proteins, such as Cry1Aa, Cry1Ab, Cry30Aa and Cry30Ca, featured different thermodynamic patterns in their DNA. Conclusion These results suggest the presence of thermodynamic variations associated to the formation of secondary structures and an evolutionary relationship with regions that encode highly conserved domains in Cry proteins. The findings of this study may have a role in the in silico design of cry gene assembly by DNA shuffling techniques.eng
dc.format.mimetypeapplication/pdfspa
dc.identifier.doi10.1186/s13628-017-0036-7spa
dc.identifier.issn2046-1682spa
dc.identifier.urihttps://repositorio.udes.edu.co/handle/001/3207spa
dc.language.isoengspa
dc.relation.ispartofBMC Biophysicseng
dc.rightsDerechos Reservados - Universidad de Santander, 2017spa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.creativecommonsAtribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)spa
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/spa
dc.sourcehttps://link.springer.com/content/pdf/10.1186%2Fs13628-017-0036-7.pdfeng
dc.subject.proposalBacillus thuringiensiseng
dc.subject.proposalCry toxinseng
dc.subject.proposalDNA shufflingeng
dc.subject.proposalDNA secondary structures in silico modelingeng
dc.titleDNA secondary structure formation by DNA shuffling of the conserved domains of the Cry protein of Bacillus thuringiensiseng
dc.typeArtículo de revistaspa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa
dc.type.contentTextspa
dc.type.driverinfo:eu-repo/semantics/articlespa
dc.type.redcolhttp://purl.org/redcol/resource_type/ARTspa
dc.type.versioninfo:eu-repo/semantics/publishedVersionspa
dspace.entity.typePublication
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2spa
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85spa
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