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dc.creatorDellarole, Mariano-
dc.creatorSánchez Miguel, Ignacio Enrique-
dc.creatorde Prat Gay, Gonzalo-
dc.date2017-03-31T15:00:42Z-
dc.date2017-03-31T15:00:42Z-
dc.date2010-12-
dc.date2017-03-29T14:46:20Z-
dc.date.accessioned2019-04-29T15:40:06Z-
dc.date.available2019-04-29T15:40:06Z-
dc.date.issued2017-03-31T15:00:42Z-
dc.date.issued2017-03-31T15:00:42Z-
dc.date.issued2010-12-
dc.date.issued2017-03-29T14:46:20Z-
dc.identifierDellarole, Mariano; Sánchez Miguel, Ignacio Enrique; de Prat Gay, Gonzalo; Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site; American Chemical Society; Biochemistry; 49; 48; 12-2010; 10277-10286-
dc.identifierhttp://hdl.handle.net/11336/14587-
dc.identifier1520-4995-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/299015-
dc.descriptionBinding cooperativity guides the formation of protein-nucleic acid complexes, in particular those that are highly regulated such as replication origins and transcription sites. Using the DNA binding domain of the origin binding and transcriptional regulator protein E2 from human papillomavirus type 16 as model, and through isothermal titration calorimetry analysis, we determined a positive, entropy-driven cooperativity upon binding of the protein to its cognate tandem double E2 site. This cooperativity is associated with a change in DNA structure, where the overall B conformation is maintained. Two homologous E2 domains, those of HPV18 and HPV11, showed that the enthalpic-entropic components of the reaction and DNA deformation can diverge. Because the DNA binding helix is almost identical in the three domains, the differences must lie dispersed throughout this unique dimeric β-barrel fold. This is in surprising agreement with previous results for this domain, which revealed a strong coupling between global dynamics and DNA recognition.-
dc.descriptionFil: Dellarole, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina-
dc.descriptionFil: Sánchez Miguel, Ignacio Enrique. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina-
dc.descriptionFil: de Prat Gay, Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherAmerican Chemical Society-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/bi1014908-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/bi1014908-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectHUMAN PAPILLOMAVIRUS-
dc.subjectORIGIN BINDING PROTEIN-
dc.subjectBINDING COOPERATIVITY-
dc.subjectISOTHERMAL TITRATION CALORIMETRY-
dc.subjectBiofísica-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleThermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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