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Título: | Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA |
Autor: | Bahia, Diana; Aviñó, Anna CSIC ORCID; Eritja Casadellà, Ramón CSIC ORCID ; Darzynkiewicz. Edward; Bach-Elias, Montse CSIC ORCID | Palabras clave: | U snRNPs UV Cross-Linking Assay Nuclear Import Snurportin 1 m3GpppG Cap Trimethylguanosine Nucleoside TMG |
Fecha de publicación: | 2006 | Editor: | Taylor & Francis | Citación: | Nucleosides, Nucleotides and Nucleic Acids 25(8): 909-923 (2006) | Resumen: | Macromolecular nuclear import is an energy-and signal-dependent process. The best characterized type of nuclear import consists of proteins carrying the classical NLS that is mediated by the heterodimeric receptor importin α/β. Spliceosomal snRNPs U1, U2, U4, and U5 nuclear import depend both on the 5' terminal m3G (trimethylguanosine) cap structure of the U snRNA and the Sm core domain. Snurportin 1 recognizes the m3G-cap structure of m3G-capped U snRNPs. In this report, we show how a synthesized trimethylguanosine nucleoside affects the binding of Snurportin 1 to m3G-capped U1 snRNA in a UV-cross-linking assay. The data indicated that TMG nucleoside is an essential component required in the recognition by Snurportin 1, thus suggesting that interaction of Snurportin 1 with U1 snRNA is not strictly dependent on the presence of the whole cap structure, but rather on the presence of the TMG nucleoside structure. These results indicate that the free nucleoside TMG could be a candidate to be an inhibitor of the interaction between Snurportin 1 and U snRNAs. We also show the behavior of free TMG nucleoside in in vitro U snRNPs nuclear import. Copyright © Taylor & Francis Group, LLC. | Versión del editor: | http://dx.doi.org/10.1080/15257770600793901 | URI: | http://hdl.handle.net/10261/109195 | DOI: | 10.1080/15257770600793901 | Identificadores: | issn: 1525-7770 e-issn: 1532-2335 |
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