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dc.contributor.author | Díaz-Moreno, Irene | - |
dc.contributor.author | García-Mayoral, M.F. | - |
dc.contributor.author | Hollingworth, David | - |
dc.contributor.author | Ramos, Andrés | - |
dc.date.accessioned | 2011-03-25T14:14:28Z | - |
dc.date.available | 2011-03-25T14:14:28Z | - |
dc.date.issued | 2008-08-06 | - |
dc.identifier.citation | Nucleic Acids Research 36(16): 5290-5296 (2008) | es_ES |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/10261/33803 | - |
dc.description | 7 páginas, 4 figuras, 1 tabla | es_ES |
dc.description.abstract | K-homology (KH) splicing regulator protein (KSRP) is a multi-domain RNA-binding protein that regulates different steps of mRNA metabolism, from mRNA splicing to mRNA decay, interacting with a broad range of RNA sequences. To understand how KSRP recognizes its different RNA targets it is necessary to define the general rules of KSRP–RNA interaction. We describe here a complete scaffold-independent analysis of the RNA-binding potential of the four KH domains of KSRP. The analysis shows that KH3 binds to the RNA with a significantly higher affinity than the other domains and recognizes specifically a G-rich target. It also demonstrates that the other KH domains of KSRP display different sequence preferences explaining the broad range of targets recognized by the protein. Further, KSRP shows a strong negative selectivity for sequences containing several adjacent Cytosines limiting the target choice of KSRP within single-stranded RNA regions. The in-depth analysis of the RNA-binding potential of the KH domains of KSRP provides us with an understanding of the role of low sequence specificity domains in RNA recognition by multi-domain RNA-binding proteins. | es_ES |
dc.description.sponsorship | The structural characterization of the KSRP–RNA interactions is supported by the Wellcome Trust Grant [grant number WT082088MA]. I.D.-M. is supported by EMBO fellowship (240-2005). Funding to pay the Open Access publication charges for this article was provided by the MRC. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Oxford University Press | es_ES |
dc.rights | openAccess | es_ES |
dc.subject | KSRP | es_ES |
dc.subject | RNA | es_ES |
dc.subject | Protein | es_ES |
dc.subject | Metabolism | es_ES |
dc.title | The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1093/nar/gkn509 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1093/nar/gkn509 | es_ES |
dc.identifier.e-issn | 1362-4962 | - |
dc.identifier.pmid | 18684992 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.languageiso639-1 | en | - |
item.fulltext | With Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | open | - |
item.openairetype | artículo | - |
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NAR_2008_36_5290.pdf | 692,99 kB | Adobe PDF | Visualizar/Abrir |
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