The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets

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...

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Autores: Díaz Moreno, Irene, García Mayoral, María Flor, Hollingworth, David, Ramos, Andrés
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2008
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/84709
Acceso en línea:https://hdl.handle.net/11441/84709
https://doi.org/10.1093/nar/gkn509
Access Level:acceso abierto
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spelling The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targetsDíaz Moreno, IreneGarcía Mayoral, María FlorHollingworth, DavidRamos, AndrésK-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.Wellcome Trust Grant WT082088MAEMBO fellowship 240-2005Oxford University PressBioquímica Vegetal y Biología Molecular2008info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/84709https://doi.org/10.1093/nar/gkn509reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésNucleic Acids Research, 36 (16), 5290-5296.WT082088MA240-2005http://dx.doi.org/10.1093/nar/gkn509info:eu-repo/semantics/openAccessoai:idus.us.es:11441/847092026-06-17T12:51:07Z
dc.title.none.fl_str_mv The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
title The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
spellingShingle The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
Díaz Moreno, Irene
title_short The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
title_full The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
title_fullStr The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
title_full_unstemmed The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
title_sort The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets
dc.creator.none.fl_str_mv Díaz Moreno, Irene
García Mayoral, María Flor
Hollingworth, David
Ramos, Andrés
author Díaz Moreno, Irene
author_facet Díaz Moreno, Irene
García Mayoral, María Flor
Hollingworth, David
Ramos, Andrés
author_role author
author2 García Mayoral, María Flor
Hollingworth, David
Ramos, Andrés
author2_role author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
description 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.
publishDate 2008
dc.date.none.fl_str_mv 2008
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/84709
https://doi.org/10.1093/nar/gkn509
url https://hdl.handle.net/11441/84709
https://doi.org/10.1093/nar/gkn509
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Nucleic Acids Research, 36 (16), 5290-5296.
WT082088MA
240-2005
http://dx.doi.org/10.1093/nar/gkn509
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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