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dc.contributor.authorBock, Lars V
dc.contributor.authorCaliskan, Neva
dc.contributor.authorKorniy, Natalia
dc.contributor.authorPeske, Frank
dc.contributor.authorRodnina, Marina V
dc.contributor.authorGrubmüller, Helmut
dc.date.accessioned2019-11-06T11:31:31Z
dc.date.available2019-11-06T11:31:31Z
dc.date.issued2019-10-10
dc.identifier.citationNat Commun. 2019 Oct 10;10(1):4598. doi: 10.1038/s41467-019-12648-x.en_US
dc.identifier.issn2041-1723
dc.identifier.pmid31601802
dc.identifier.doi10.1038/s41467-019-12648-x
dc.identifier.urihttp://hdl.handle.net/10033/622005
dc.description.abstractmRNA contexts containing a 'slippery' sequence and a downstream secondary structure element stall the progression of the ribosome along the mRNA and induce its movement into the -1 reading frame. In this study we build a thermodynamic model based on Bayesian statistics to explain how -1 programmed ribosome frameshifting can work. As training sets for the model, we measured frameshifting efficiencies on 64 dnaX mRNA sequence variants in vitro and also used 21 published in vivo efficiencies. With the obtained free-energy difference between mRNA-tRNA base pairs in the 0 and -1 frames, the frameshifting efficiency of a given sequence can be reproduced and predicted from the tRNA-mRNA base pairing in the two frames. Our results further explain how modifications in the tRNA anticodon modulate frameshifting and show how the ribosome tunes the strength of the base-pair interactions.en_US
dc.publisherNature Researchen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleThermodynamic control of -1 programmed ribosomal frameshifting.en_US
dc.typeArticleen_US
dc.contributor.departmentHIRI, Helmholtz-Institut für RNA-basierte Infektionsforschung, Josef-Shneider Strasse 2, 97080 Würzburg, Germany.en_US
dc.identifier.journalNature Communicationsen_US
refterms.dateFOA2019-11-06T11:31:31Z
dc.source.journaltitleNature communications


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