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dc.contributor.author | Toribio, René | |
dc.contributor.author | Díaz-López, Irene | |
dc.contributor.author | Boskovic, Jasminka | |
dc.contributor.author | Ventoso, Ivan | |
dc.date.accessioned | 2018-10-23T12:17:53Z | |
dc.date.available | 2018-10-23T12:17:53Z | |
dc.date.issued | 2018-05-04 | |
dc.identifier.citation | Nucleic Acids Res. 2018; 46 (8): 4176-4187. | es_ES |
dc.identifier.issn | 0305-1048 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/6503 | |
dc.description.abstract | The topology and dynamics of the scanning ribosomal 43S pre-initiation complex (PIC) bound to mRNA and initiation factors (eIFs) are probably the least understood aspects of translation initiation in eukaryotes. Recently, we described a trapping mechanism in alphavirus that stalls the PIC during scanning of viral mRNA. Using this model, we were able to snapshot for the first time the eIF4A helicase bound to mRNA in a 48S initiation complex assembled in vitro. This interaction was only detected in the presence of the natural stem loop structure (DLP) located downstream from the AUG in viral mRNA that promoted stalling of the PIC, suggesting that DLP stability was enough to jam the helicase activity of eIF4A in a fraction of assembled 48S complexes. However, a substantial proportion of DLP mRNA molecules were effectively unwound by eIF4A in vitro, an activity that alphaviruses counteract in infected cells by excluding eIF4A from viral factories. Our data indicated that eIF4A-mRNA contact occurred in (or near) the ES6S region of the 40S subunit, suggesting that incoming mRNA sequences penetrate through the ES6S region during the scanning process. We propose a topological model of the scanning PIC and how some viruses have exploited this topology to translate their mRNAs with fewer eIF requirements. | es_ES |
dc.description.sponsorship | We are indebted to Jerry Pelletier (McGill University) for providing us with hippuristanol. We also thank the Genomics Facility at the López Neira Institute (Granada, Spain) for efficient analysis of toeprinting products, and the Electron Microscopy facility of the CBMSO for negative staining EM. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Oxford University Press | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject | 43S PREINITIATION COMPLEX | es_ES |
dc.subject | SECONDARY STRUCTURE | es_ES |
dc.subject | HELICASE ACTIVITY | es_ES |
dc.subject | CODON SELECTION | es_ES |
dc.subject | FACTOR 4A | es_ES |
dc.subject | FACTOR 4G | es_ES |
dc.subject | EIF4A | es_ES |
dc.subject | MECHANISM | es_ES |
dc.subject | RIBOSOME | es_ES |
dc.subject | INHIBITION | es_ES |
dc.title | Translation initiation of alphavirus mRNA reveals new insights into the topology of the 48S initiation complex | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución-NoComercial-CompartirIgual 4.0 Internacional | * |
dc.identifier.pubmedID | 29415133 | es_ES |
dc.format.volume | 46 | es_ES |
dc.format.number | 8 | es_ES |
dc.format.page | 4176-4187 | es_ES |
dc.identifier.doi | 10.1093/nar/gky071 | es_ES |
dc.contributor.funder | Ministerio de Ciencia e Innovación (España) | |
dc.description.peerreviewed | Sí | |
dc.identifier.e-issn | 1362-4962 | es_ES |
dc.relation.publisherversion | https://doi.org/10.1093/nar/gky071 | es_ES |
dc.identifier.journal | Nucleic acids research | es_ES |
dc.repisalud.institucion | CNIO | es_ES |
dc.repisalud.orgCNIO | CNIO::Grupos de investigación | es_ES |
dc.repisalud.orgCNIO | CNIO::Unidades técnicas::Unidad de Microscopía Electrónica | es_ES |
dc.relation.projectID | info:eu-repo/gratAgreement/ES/BFU2013-4005R | es_ES |
dc.rights.accessRights | open access | es_ES |