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http://hdl.handle.net/10261/161177
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Canales, Ángeles | es_ES |
dc.contributor.author | Rösinger, Marcel | es_ES |
dc.contributor.author | Sastre, Javier | es_ES |
dc.contributor.author | Felli, Isabella C. | es_ES |
dc.contributor.author | Jiménez-Barbero, Jesús | es_ES |
dc.contributor.author | Giménez-Gallego, Guillermo | es_ES |
dc.contributor.author | Fernández-Tornero, Carlos | es_ES |
dc.date.accessioned | 2018-02-22T09:53:46Z | - |
dc.date.available | 2018-02-22T09:53:46Z | - |
dc.date.issued | 2017-12-06 | - |
dc.identifier.citation | PLoS ONE 12(12): e0189171 (2017) | es_ES |
dc.identifier.uri | http://hdl.handle.net/10261/161177 | - |
dc.description | 15 p.-6 fig. | es_ES |
dc.description.abstract | C/EBP-homologous protein (CHOP) is a key determinant of the apoptotic response to endoplasmic reticulum stress or DNA damage. As a member of the C/EBP family, CHOP contains a low complexity N-terminal region involved in transcriptional activation, followed by a bZIP that binds DNA after dimerization. However, in contrast to other C/EBPs, CHOP directs binding to non-canonical C/EBP sites due to unique substitutions in its DNA-binding domain. Herein, we show that the N-terminal region of CHOP is intrinsically unstructured but contains two segments presenting α-helical propensity. One of these segments is conserved in other C/EBPs and mediates essential roles of CHOP, including regulation through phosphorylation. The second segment is placed within a proteolytic-resistant portion of the protein and exhibits reduced flexibility. Moreover, the DNA-binding region of CHOP also contains a segment with α-helical character towards its most N-terminal part. Our results suggest that structure-prone segments scattered within disordered regions may be critical for macromolecular recognition during CHOP-mediated transcriptional activation. | es_ES |
dc.description.sponsorship | This work was supported by the Spanish Ministry of Economy and Competitiveness [BFU2013-48374-P to C.F.-T., CTQ2016-76263-P to A.C.]; the Ramón Areces Foundation [to C.F.-T.]; and the European Commission [BioNMR (Contract No. 261863) to I.C.F.]. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Public Library of Science | es_ES |
dc.relation | info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2013-48374-P | es_ES |
dc.relation | info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2016-76263-P | es_ES |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/261863 | es_ES |
dc.relation.isversionof | Publisher's version | es_ES |
dc.rights | openAccess | es_ES |
dc.title | Hidden α-helical propensity segments within disordered regions of the transcriptional activator CHOP | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1371/journal.pone.0189171 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | https://doi.org/10.1371/journal.pone.0189171 | es_ES |
dc.identifier.e-issn | 1932-6203 | - |
dc.rights.license | https://creativecommons.org/licenses/by/4.0/ | es_ES |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | es_ES |
dc.contributor.funder | Fundación Ramón Areces | es_ES |
dc.contributor.funder | European Commission | es_ES |
dc.relation.csic | Sí | es_ES |
oprm.item.hasRevision | no ko 0 false | * |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100000780 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.identifier.pmid | 29211802 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.languageiso639-1 | en | - |
item.fulltext | With Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | open | - |
item.openairetype | artículo | - |
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Plos_One_Canales_2017.pdf | Artículo principal | 1,71 MB | Adobe PDF | Visualizar/Abrir |
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