Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras

RNA-binding proteins (RBPs) commonly feature multiple RNA-binding domains (RBDs), which provide these proteins with a modular architecture. Accumulating evidence supports that RBP architectural modularity and adaptability define the specificity of their interactions with RNA. However, how multiple R...

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Detalles Bibliográficos
Autores: Hollmann, Nele Merret, Jagtap, Pravin Kumar Ankush, Masiewicz, Pawel, Guitart, Tanit, Simon, Bernd, Provaznik, Jan, Stein, Frank, Haberkant, Per, Sweetapple, Lara Jayne, Villacorta, Laura, Mooijman, Dylan, Benes, Vladimir, Savitski, Mikhail M., Gebauer, Fátima, Hennig, Janosch
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/45504
Acceso en línea:http://hdl.handle.net/10230/45504
http://dx.doi.org/10.1016/j.celrep.2020.107930
Access Level:acceso abierto
Palabra clave:NMR spectroscopy
RNA-binding domains
RNA-binding proteins
Cold-shock domains
Integrative structural biology
Ribonucleoproteins
Translation regulation
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spelling Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-RasHollmann, Nele MerretJagtap, Pravin Kumar AnkushMasiewicz, PawelGuitart, TanitSimon, BerndProvaznik, JanStein, FrankHaberkant, PerSweetapple, Lara JayneVillacorta, LauraMooijman, DylanBenes, VladimirSavitski, Mikhail M.Gebauer, FátimaHennig, JanoschNMR spectroscopyRNA-binding domainsRNA-binding proteinsCold-shock domainsIntegrative structural biologyRibonucleoproteinsTranslation regulationRNA-binding proteins (RBPs) commonly feature multiple RNA-binding domains (RBDs), which provide these proteins with a modular architecture. Accumulating evidence supports that RBP architectural modularity and adaptability define the specificity of their interactions with RNA. However, how multiple RBDs recognize their cognate single-stranded RNA (ssRNA) sequences in concert remains poorly understood. Here, we use Upstream of N-Ras (Unr) as a model system to address this question. Although reported to contain five ssRNA-binding cold-shock domains (CSDs), we demonstrate that Unr includes an additional four CSDs that do not bind RNA (pseudo-RBDs) but are involved in mediating RNA tertiary structure specificity by reducing the conformational heterogeneity of Unr. Disrupting the interactions between canonical and non-canonical CSDs impacts RNA binding, Unr-mediated translation regulation, and the Unr-dependent RNA interactome. Taken together, our studies reveal a new paradigm in protein-RNA recognition, where interactions between RBDs and pseudo-RBDs select RNA tertiary structures, influence RNP assembly, and define target specificity.Elsevier202020202020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/45504http://dx.doi.org/10.1016/j.celrep.2020.107930reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésCell Rep. 2020; 32(3):107930© 2020 The Authors. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).http://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:recercat.cat:10230/455042026-05-29T05:05:01Z
dc.title.none.fl_str_mv Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
title Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
spellingShingle Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
Hollmann, Nele Merret
NMR spectroscopy
RNA-binding domains
RNA-binding proteins
Cold-shock domains
Integrative structural biology
Ribonucleoproteins
Translation regulation
title_short Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
title_full Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
title_fullStr Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
title_full_unstemmed Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
title_sort Pseudo-RNA-binding domains mediate RNA structure specificity in upstream of N-Ras
dc.creator.none.fl_str_mv Hollmann, Nele Merret
Jagtap, Pravin Kumar Ankush
Masiewicz, Pawel
Guitart, Tanit
Simon, Bernd
Provaznik, Jan
Stein, Frank
Haberkant, Per
Sweetapple, Lara Jayne
Villacorta, Laura
Mooijman, Dylan
Benes, Vladimir
Savitski, Mikhail M.
Gebauer, Fátima
Hennig, Janosch
author Hollmann, Nele Merret
author_facet Hollmann, Nele Merret
Jagtap, Pravin Kumar Ankush
Masiewicz, Pawel
Guitart, Tanit
Simon, Bernd
Provaznik, Jan
Stein, Frank
Haberkant, Per
Sweetapple, Lara Jayne
Villacorta, Laura
Mooijman, Dylan
Benes, Vladimir
Savitski, Mikhail M.
Gebauer, Fátima
Hennig, Janosch
author_role author
author2 Jagtap, Pravin Kumar Ankush
Masiewicz, Pawel
Guitart, Tanit
Simon, Bernd
Provaznik, Jan
Stein, Frank
Haberkant, Per
Sweetapple, Lara Jayne
Villacorta, Laura
Mooijman, Dylan
Benes, Vladimir
Savitski, Mikhail M.
Gebauer, Fátima
Hennig, Janosch
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv NMR spectroscopy
RNA-binding domains
RNA-binding proteins
Cold-shock domains
Integrative structural biology
Ribonucleoproteins
Translation regulation
topic NMR spectroscopy
RNA-binding domains
RNA-binding proteins
Cold-shock domains
Integrative structural biology
Ribonucleoproteins
Translation regulation
description RNA-binding proteins (RBPs) commonly feature multiple RNA-binding domains (RBDs), which provide these proteins with a modular architecture. Accumulating evidence supports that RBP architectural modularity and adaptability define the specificity of their interactions with RNA. However, how multiple RBDs recognize their cognate single-stranded RNA (ssRNA) sequences in concert remains poorly understood. Here, we use Upstream of N-Ras (Unr) as a model system to address this question. Although reported to contain five ssRNA-binding cold-shock domains (CSDs), we demonstrate that Unr includes an additional four CSDs that do not bind RNA (pseudo-RBDs) but are involved in mediating RNA tertiary structure specificity by reducing the conformational heterogeneity of Unr. Disrupting the interactions between canonical and non-canonical CSDs impacts RNA binding, Unr-mediated translation regulation, and the Unr-dependent RNA interactome. Taken together, our studies reveal a new paradigm in protein-RNA recognition, where interactions between RBDs and pseudo-RBDs select RNA tertiary structures, influence RNP assembly, and define target specificity.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
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 http://hdl.handle.net/10230/45504
http://dx.doi.org/10.1016/j.celrep.2020.107930
url http://hdl.handle.net/10230/45504
http://dx.doi.org/10.1016/j.celrep.2020.107930
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Cell Rep. 2020; 32(3):107930
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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