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Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3

dc.contributor.authorBeißel, Christian
dc.contributor.authorNeumann, Bettina
dc.contributor.authorUhse, Simon
dc.contributor.authorHampe, Irene
dc.contributor.authorKarki, Prajwal
dc.contributor.authorKrebber, Heike
dc.date.accessioned2019-07-25T10:26:22Z
dc.date.available2019-07-25T10:26:22Z
dc.date.issued2019de
dc.relation.ISSN1362-4962de
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/16303
dc.description.abstractTranslation termination requires eRF1 and eRF3 for polypeptide- and tRNA-release on stop codons. Additionally, Dbp5/DDX19 and Rli1/ABCE1 are required; however, their function in this process is currently unknown. Using a combination of in vivo and in vitro experiments, we show that they regulate a stepwise assembly of the termination complex. Rli1 and eRF3-GDP associate with the ribosome first. Subsequently, Dbp5-ATP delivers eRF1 to the stop codon and in this way prevents a premature access of eRF3. Dbp5 dissociates upon placing eRF1 through ATP-hydrolysis. This in turn enables eRF1 to contact eRF3, as the binding of Dbp5 and eRF3 to eRF1 is mutually exclusive. Defects in the Dbp5-guided eRF1 delivery lead to premature contact and premature dissociation of eRF1 and eRF3 from the ribosome and to subsequent stop codon readthrough. Thus, the stepwise Dbp5-controlled termination complex assembly is essential for regular translation termination events. Our data furthermore suggest a possible role of Dbp5/DDX19 in alternative translation termination events, such as during stress response or in developmental processes, which classifies the helicase as a potential drug target for nonsense suppression therapy to treat cancer and neurodegenerative diseases.de
dc.description.sponsorshipOpen-Access-Publikationsfonds 2019
dc.language.isoengde
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectribosomal entry; eRF1; eRF3de
dc.subject.ddc570
dc.titleTranslation termination depends on the sequential ribosomal entry of eRF1 and eRF3de
dc.typejournalArticlede
dc.identifier.doi10.1093/nar/gkz177
dc.type.versionpublishedVersionde
dc.relation.pISSN0305-1048
dc.relation.eISSN1362-4962
dc.bibliographicCitation.volume47de
dc.bibliographicCitation.issue9de
dc.bibliographicCitation.firstPage4798de
dc.bibliographicCitation.lastPage4813de
dc.type.subtypejournalArticle
dc.identifier.pmid30873535
dc.description.statuspeerReviewedde
dc.bibliographicCitation.journalNucleic Acids Researchde


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