dc.creator | González Arzola, Katiuska | es |
dc.creator | Guerra Castellano, Alejandra | es |
dc.creator | Rivero Rodríguez, Francisco | es |
dc.creator | Casado Combreras, Miguel Ángel | es |
dc.creator | Pérez Mejías, Gonzalo | es |
dc.creator | Díaz Quintana, Antonio Jesús | es |
dc.creator | Díaz Moreno, Irene | es |
dc.creator | Rosa Acosta, Miguel Ángel de la | es |
dc.date.accessioned | 2021-06-04T13:48:09Z | |
dc.date.available | 2021-06-04T13:48:09Z | |
dc.date.issued | 2021 | |
dc.identifier.citation | González Arzola, K., Guerra Castellano, A., Rivero Rodríguez, F., Casado Combreras, M.Á., Pérez Mejías, G., Díaz Quintana, A.J.,...,Rosa Acosta, M.Á.d.l. (2021). Mitochondrial cytochrome c shot towards histone chaperone condensates in the nucleus. FEBS Open Bio | |
dc.identifier.issn | 2211-5463 | es |
dc.identifier.uri | https://hdl.handle.net/11441/111397 | |
dc.description.abstract | Despite mitochondria being key for the control of cell homeostasis and fate, their role in DNA damage response is usually just regarded as an apoptotic trigger. However, growing evidence points to mitochondrial factors modulating nuclear functions. Remarkably, after DNA damage, cytochrome c (Cc) interacts in the cell nucleus with a variety of well-known histone chaperones, whose activity is competitively inhibited by the haem protein. As nuclear Cc inhibits the nucleosome assembly/disassembly activity of histone chaperones, it might indeed affect chromatin dynamics and histone deposition on DNA. Several histone chaperones actually interact with Cc Lys residues through their acidic regions, which are also involved in heterotypic interactions leading to liquid–liquid phase transitions responsible for the assembly of nuclear condensates, including heterochromatin. This relies on dynamic histone–DNA interactions that can be modulated by acetylation of specific histone Lys residues. Thus, Cc may have a major regulatory role in DNA repair by fine-tuning nucleosome assembly activity and likely nuclear condensate formation. | es |
dc.description.sponsorship | Ministerio de Ciencia, Innovación y Universidades PGC2018-096049-B-I00 | es |
dc.description.sponsorship | Junta de Andalucía BIO198, US-1254317, US-1257019, P18-FR-3487, P18-HO-4091 | es |
dc.format | application/pdf | es |
dc.format.extent | 23 p. | es |
dc.language.iso | eng | es |
dc.publisher | Wiley-Blackwell | es |
dc.relation.ispartof | FEBS Open Bio | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Chromatin remodelling | es |
dc.subject | Cytochrome c | es |
dc.subject | DNA damage response | es |
dc.subject | Histone chaperone | es |
dc.subject | Liquid–liquid phase separation | es |
dc.subject | Lysine acetylation | es |
dc.title | Mitochondrial cytochrome c shot towards histone chaperone condensates in the nucleus | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.projectID | PGC2018-096049-B-I00 | es |
dc.relation.projectID | BIO198 | es |
dc.relation.projectID | US-1254317 | es |
dc.relation.projectID | US-1257019 | es |
dc.relation.projectID | P18-FR-3487 | es |
dc.relation.projectID | P18-HO-4091 | es |
dc.relation.publisherversion | https://doi.org/10.1002/2211-5463.13176 | es |
dc.identifier.doi | 10.1002/2211-5463.13176 | es |
dc.journaltitle | FEBS Open Bio | es |