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dc.contributor.authorVelasco, Lara Franciele Ribeiro-
dc.contributor.authorTogashi, Marie-
dc.contributor.authorWalfish, Paul G.-
dc.contributor.authorPessanha, Rutnéia de Paula-
dc.contributor.authorMoura, Fanny Nascimento-
dc.contributor.authorBarra, Gustavo Barcelos-
dc.contributor.authorNguyen, Phuong-
dc.contributor.authorRebong, Rachelle-
dc.contributor.authorYuan, Chaoshen-
dc.contributor.authorSimeoni, Luiz Alberto-
dc.contributor.authorRibeiro, Ralff Carvalho Justiniano-
dc.contributor.authorBaxter, John Darling-
dc.contributor.authorWebb, Paul-
dc.contributor.authorNeves, Francisco de Assis Rocha-
dc.date.accessioned2013-05-22T18:32:09Z-
dc.date.available2013-05-22T18:32:09Z-
dc.date.issued2007-04-
dc.identifier.citationVELASCO, Lara F. R. et al. Thyroid hormone response element organization dictates the composition of active receptor. The Journal of Biological Chemistry, EUA, v. 282, n. 17, Apr. 2007. Disponível em: <http://www.jbc.org/content/282/17/12458.full.pdf+html?sid=8173e574-01d4-4ac4-9fca-71f7558f7599>. Acesso em: 20 maio 2013. DOI: 10.1074/jbc.M610700200.en
dc.identifier.urihttp://repositorio.unb.br/handle/10482/13180-
dc.description.abstractThyroid hormone (triiodothyronine, T3) is known to activate transcription by binding heterodimers of thyroid hormone receptors (TRs) and retinoid X receptors (RXRs). RXR-TRs bind to T3 response elements (TREs) composed of direct repeats of the sequence AGGTCA spaced by four nucleotides (DR-4). In other TREs, however, the half-sites can be arranged as inverted palindromes and palindromes (Pal). Here we show that TR homodimers and monomers activate transcription from representative TREs with alternate half-site placements. TRβ activates transcription more efficiently than TRα at an inverted palindrome (F2), and this correlates with preferential TRβ homodimer formation at F2 in vitro. Furthermore, reconstruction of TR transcription complexes in yeast indicates that TRβ homodimers are active at F2, whereas RXR-TRs are active at DR-4 and Pal. Finally, analysis of TRβ mutations that block homodimer and/or heterodimer formation reveal TRE-selective requirements for these surfaces in mammalian cells, which suggest that TRβ homodimers are active at F2, RXR-TRs at DR-4, and TR monomers at Pal. TRβ requires higher levels of hormone for activation at F2 than other TREs, and this differential effect is abolished by a dimer surface mutation suggesting that it is related to composition of the TR·TRE complex. We propose that interactions of particular TR oligomers with different elements play unappreciated roles in TRE-selective actions of liganded TRs in vivo.en
dc.language.isoInglêsen
dc.publisherThe American Society for Biochemistry and Molecular Biology, Inc.en
dc.rightsAcesso Abertoen
dc.titleThyroid hormone response element organization dictates the composition of active receptoren
dc.typeArtigoen
dc.subject.keywordTireóide - hormôniosen
dc.subject.keywordReceptor do hormônio tireoideanoen
dc.subject.keywordTireóideen
dc.rights.licenseThe Journal of Biological Chemistry - Authors need NOT contact the journal to obtain rights to reuse their own material. They are automatically granted permission to do the following: Reproduce an article for use in the author's courses. (If the author is employed by an academic institution, that institution also may reproduce the article for teaching purposes.). Fonte: http://www.jbc.org/site/misc/Copyright_Permission.xhtml. Acesso em: 20 maio 2013.en
dc.identifier.doihttps://dx.doi.org/10.1074/jbc.M610700200en
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