Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA

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...

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Detalles Bibliográficos
Autores: Bahia, Diana, Aviñó, Anna, Eritja Casadellà, Ramón, Darzynkiewicz. Edward, Bach-Elias, Montse
Tipo de recurso: artículo
Fecha de publicación:2006
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/109195
Acceso en línea:http://hdl.handle.net/10261/109195
Access Level:acceso abierto
Palabra clave:U snRNPs
UV Cross-Linking Assay
Nuclear Import
Snurportin 1
m3GpppG Cap
Trimethylguanosine Nucleoside
TMG
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spelling Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNABahia, DianaAviñó, AnnaEritja Casadellà, RamónDarzynkiewicz. EdwardBach-Elias, MontseU snRNPsUV Cross-Linking AssayNuclear ImportSnurportin 1m3GpppG CapTrimethylguanosine NucleosideTMGMacromolecular 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.This work was supported by Plan Nacional BFU2005-00701 and the Polish Committee for Scientific Research (KBN) # 6 P04A 055 17. D.B. was a recipient of a CNPq Brazilian fellowship and EMBO and FEBS short-term fellowshipsPeer ReviewedTaylor & FrancisMinisterio de Educación y Ciencia (España)State Committee for Scientific Research (Poland)Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2015201520062015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/109195reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1080/15257770600793901Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1091952026-05-22T06:33:51Z
dc.title.none.fl_str_mv Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
title Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
spellingShingle Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
Bahia, Diana
U snRNPs
UV Cross-Linking Assay
Nuclear Import
Snurportin 1
m3GpppG Cap
Trimethylguanosine Nucleoside
TMG
title_short Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
title_full Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
title_fullStr Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
title_full_unstemmed Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
title_sort Trimethylguanosine nucleoside inhibits cross-linking between snurportin 1 and m3G-capped U1 snRNA
dc.creator.none.fl_str_mv Bahia, Diana
Aviñó, Anna
Eritja Casadellà, Ramón
Darzynkiewicz. Edward
Bach-Elias, Montse
author Bahia, Diana
author_facet Bahia, Diana
Aviñó, Anna
Eritja Casadellà, Ramón
Darzynkiewicz. Edward
Bach-Elias, Montse
author_role author
author2 Aviñó, Anna
Eritja Casadellà, Ramón
Darzynkiewicz. Edward
Bach-Elias, Montse
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Educación y Ciencia (España)
State Committee for Scientific Research (Poland)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv U snRNPs
UV Cross-Linking Assay
Nuclear Import
Snurportin 1
m3GpppG Cap
Trimethylguanosine Nucleoside
TMG
topic U snRNPs
UV Cross-Linking Assay
Nuclear Import
Snurportin 1
m3GpppG Cap
Trimethylguanosine Nucleoside
TMG
description 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.
publishDate 2006
dc.date.none.fl_str_mv 2006
2015
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/109195
url http://hdl.handle.net/10261/109195
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1080/15257770600793901
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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