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dc.contributor.authorWaris, Sabooraes_ES
dc.contributor.authorGarcía-Mauriño, Sofía M.es_ES
dc.contributor.authorSivakumaran, Andrewes_ES
dc.contributor.authorBeckham, Simone A.es_ES
dc.contributor.authorLoughlin, Fionna E.es_ES
dc.contributor.authorGorospe, Myriames_ES
dc.contributor.authorDíaz-Moreno, Irenees_ES
dc.contributor.authorWilce, Matthew C.J.es_ES
dc.contributor.authorWilce, Jacqueline A.es_ES
dc.date.accessioned2017-05-19T11:04:15Z-
dc.date.available2017-05-19T11:04:15Z-
dc.date.issued2017-
dc.identifier.citationNucleic Acids Research, 45(8):4944-4957 (2017)es_ES
dc.identifier.urihttp://hdl.handle.net/10261/150024-
dc.description.abstractTIA-1 (T-cell restricted intracellular antigen-1) is an RNA-binding protein involved in splicing and translational repression. It mainly interacts with RNA via its second and third RNA recognition motifs (RRMs), with specificity for U-rich sequences directed by RRM2. It has recently been shown that RRM3 also contributes to binding, with preferential binding for C-rich sequences. Here we designed UC-rich and CU-rich 10-nt sequences for engagement of both RRM2 and RRM3 and demonstrated that the TIA-1 RRM23 construct preferentially binds the UC-rich RNA ligand (5΄-UUUUUACUCC-3΄). Interestingly, this binding depends on the presence of Lys274 that is C-terminal to RRM3 and binding to equivalent DNA sequences occurs with similar affinity. Small-angle X-ray scattering was used to demonstrate that, upon complex formation with target RNA or DNA, TIA-1 RRM23 adopts a compact structure, showing that both RRMs engage with the target 10-nt sequences to form the complex. We also report the crystal structure of TIA-1 RRM2 in complex with DNA to 2.3 Å resolution providing the first atomic resolution structure of any TIA protein RRM in complex with oligonucleotide. Together our data support a specific mode of TIA-1 RRM23 interaction with target oligonucleotides consistent with the role of TIA-1 in binding RNA to regulate gene expression.es_ES
dc.language.isoenges_ES
dc.publisherOxford University Presses_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccesses_ES
dc.titleTIA-1 RRM23 binding and recognition of target oligonucleotideses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1093/nar/gkx102-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1093/nar/gkx102es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
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