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Artículo
TIA-1 RRM23 binding and recognition of target oligonucleotides
dc.creator | Waris, Saboora | es |
dc.creator | García Mauriño, Sofía M. | es |
dc.creator | Sivakumaran, Andrew | es |
dc.creator | Díaz Moreno, Irene | es |
dc.date.accessioned | 2017-06-01T10:13:31Z | |
dc.date.available | 2017-06-01T10:13:31Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Waris, S., García Mauriño, S.M., Sivakumaran, A. y Díaz Moreno, I. (2017). TIA-1 RRM23 binding and recognition of target oligonucleotides. Nucleic Acids Research, 45 (8), 49448-84957. | |
dc.identifier.issn | 0305-1048 | es |
dc.identifier.uri | http://hdl.handle.net/11441/60725 | |
dc.description.abstract | TIA-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 |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation.ispartof | Nucleic Acids Research, 45 (8), 49448-84957. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | TIA-1 RRM23 binding and recognition of target oligonucleotides | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Biología Vegetal y Ecología | es |
dc.relation.publisherversion | http://dx.doi.org/10.1093/nar/gkx102 | es |
dc.identifier.doi | 10.1093/nar/gkx102 | es |
idus.format.extent | 10 p. | es |
dc.journaltitle | Nucleic Acids Research | es |
dc.publication.volumen | 45 | es |
dc.publication.issue | 8 | es |
dc.publication.initialPage | 49448 | es |
dc.publication.endPage | 84957 | es |
Ficheros | Tamaño | Formato | Ver | Descripción |
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pub5gkx102.pdf | 4.529Mb | [PDF] | Ver/ | |