dc.creator | Hohl, Marcel | es |
dc.creator | Muñoz Galván, Sandra | es |
dc.creator | Tous Rivera, Cristina | es |
dc.creator | Aguilera López, Andrés | es |
dc.creator | Petrini, John H. J. | es |
dc.date.accessioned | 2018-03-19T17:44:45Z | |
dc.date.available | 2018-03-19T17:44:45Z | |
dc.date.issued | 2011 | |
dc.identifier.citation | Hohl, M., Muñoz Galván, S., Tous Rivera, C., Aguilera López, A. y Petrini, J.H.J. (2011). The Rad50 coiled-coil domain is indispensable for Mre11 complex functions. Nature Structural and Molecular Biology, 18 (10), 1124-1131. | |
dc.identifier.issn | 1545-9993 (impreso) | es |
dc.identifier.issn | 1545-9985 (electrónico) | es |
dc.identifier.uri | https://hdl.handle.net/11441/71104 | |
dc.description.abstract | The Mre11 complex (Mre11, Rad50 and Xrs2 in Saccharomyces cerevisiae) influences diverse functions in the DNA damage response. The complex comprises the globular DNA-binding domain and the Rad50 hook domain, which are linked by a long and extended Rad50 coiled-coil domain. In this study, we constructed rad50 alleles encoding truncations of the coiled-coil domain to determine which Mre11 complex functions required the full length of the coils. These mutations abolished telomere maintenance and meiotic double-strand break (DSB) formation, and severely impaired homologous recombination, indicating a requirement for long-range action. Nonhomologous end joining, which is probably mediated by the globular domain of the Mre11 complex, was also severely impaired by alteration of the coiled-coil and hook domains, providing the first evidence of their influence on this process. These data show that functions of Mre11 complex are integrated by the coiled coils of Rad50. | es |
dc.description.sponsorship | Swiss National Science Foundation and Eugen and Elisabeth Schellenberg Foundation GM56888, PBZH33-112756, PA0033-117484 | es |
dc.description.sponsorship | Ministerio de Ciencia e Innovación BFU2006-05260, 2010 CSD2007-015 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Nature Publishing Group | es |
dc.relation.ispartof | Nature Structural and Molecular Biology, 18 (10), 1124-1131. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | DNA repair | es |
dc.subject | Mre11 complex | es |
dc.subject | Rad50 | es |
dc.subject | Hook | es |
dc.subject | DNA double strand break | es |
dc.subject | Coiled coil | es |
dc.title | The Rad50 coiled-coil domain is indispensable for Mre11 complex functions | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/submittedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Genética | es |
dc.relation.projectID | GM56888 | es |
dc.relation.projectID | PBZH33-112756 | es |
dc.relation.projectID | PA0033-117484 | es |
dc.relation.projectID | BFU2006-05260 | es |
dc.relation.projectID | 2010 CSD2007-015 | es |
dc.relation.publisherversion | http://dx.doi.org/10.1038/nsmb.2116 | es |
dc.identifier.doi | 10.1038/nsmb.2116 | es |
idus.format.extent | 21 p. | es |
dc.journaltitle | Nature Structural and Molecular Biology | es |
dc.publication.volumen | 18 | es |
dc.publication.issue | 10 | es |
dc.publication.initialPage | 1124 | es |
dc.publication.endPage | 1131 | es |
dc.contributor.funder | Swiss National Science Foundation (SNFS) | |
dc.contributor.funder | Ministerio de Ciencia e Innovación (MICIN). España | |