Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis

Autores
Esteve Bruna, David; Carrasco López, Cristian; Blanco Touriñán, Noel; Iserte, Javier Alonso; Calleja Cabrera, Julián; Perea Resa, Carlos; Úrbez, Cristina; Carrasco, Pedro; Yanovsky, Marcelo Javier; Blázquez, Miguel A.; Salinas, Julio; Alabadí, David
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Although originally identified as the components of the complex aiding the cytosolic chaperonin CCT in the folding of actins and tubulins in the cytosol, prefoldins (PFDs) are emerging as novel regulators influencing gene expression in the nucleus. Work conducted mainly in yeast and animals showed that PFDs act as transcriptional regulators and participate in the nuclear proteostasis. To investigate new functions of PFDs, we performed a co-expression analysis in Arabidopsis thaliana. Results revealed co-expression between PFD and the Sm-like (LSM) genes, which encode the LSM2–8 spliceosome core complex, in this model organism. Here, we show that PFDs interact with and are required to maintain adequate levels of the LSM2–8 complex. Our data indicate that levels of the LSM8 protein, which defines and confers the functional specificity of the complex, are reduced in pfd mutants and in response to the Hsp90 inhibitor geldanamycin. We provide biochemical evidence showing that LSM8 is a client of Hsp90 and that PFD4 mediates the interaction between both proteins. Consistent with our results and with the role of the LSM2–8 complex in splicing through the stabilization of the U6 snRNA, pfd mutants showed reduced levels of this snRNA and altered pre-mRNA splicing patterns.
Fil: Esteve Bruna, David. Universidad Politécnica de Valencia; España
Fil: Carrasco López, Cristian. Consejo Superior de Investigaciones Científicas; España
Fil: Blanco Touriñán, Noel. Universidad Politécnica de Valencia; España
Fil: Iserte, Javier Alonso. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Calleja Cabrera, Julián. Universidad Politécnica de Valencia; España
Fil: Perea Resa, Carlos. Consejo Superior de Investigaciones Científicas; España
Fil: Úrbez, Cristina. Universidad Politécnica de Valencia; España
Fil: Carrasco, Pedro. Universidad Politécnica de Valencia; España
Fil: Yanovsky, Marcelo Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Blázquez, Miguel A.. Universidad Politécnica de Valencia; España
Fil: Salinas, Julio. Consejo Superior de Investigaciones Científicas; España
Fil: Alabadí, David. Universidad Politécnica de Valencia; España
Materia
LSM2-8 complex
prefoldins
spliceosome
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/138711

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in ArabidopsisEsteve Bruna, DavidCarrasco López, CristianBlanco Touriñán, NoelIserte, Javier AlonsoCalleja Cabrera, JuliánPerea Resa, CarlosÚrbez, CristinaCarrasco, PedroYanovsky, Marcelo JavierBlázquez, Miguel A.Salinas, JulioAlabadí, DavidLSM2-8 complexprefoldinsspliceosomehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Although originally identified as the components of the complex aiding the cytosolic chaperonin CCT in the folding of actins and tubulins in the cytosol, prefoldins (PFDs) are emerging as novel regulators influencing gene expression in the nucleus. Work conducted mainly in yeast and animals showed that PFDs act as transcriptional regulators and participate in the nuclear proteostasis. To investigate new functions of PFDs, we performed a co-expression analysis in Arabidopsis thaliana. Results revealed co-expression between PFD and the Sm-like (LSM) genes, which encode the LSM2–8 spliceosome core complex, in this model organism. Here, we show that PFDs interact with and are required to maintain adequate levels of the LSM2–8 complex. Our data indicate that levels of the LSM8 protein, which defines and confers the functional specificity of the complex, are reduced in pfd mutants and in response to the Hsp90 inhibitor geldanamycin. We provide biochemical evidence showing that LSM8 is a client of Hsp90 and that PFD4 mediates the interaction between both proteins. Consistent with our results and with the role of the LSM2–8 complex in splicing through the stabilization of the U6 snRNA, pfd mutants showed reduced levels of this snRNA and altered pre-mRNA splicing patterns.Fil: Esteve Bruna, David. Universidad Politécnica de Valencia; EspañaFil: Carrasco López, Cristian. Consejo Superior de Investigaciones Científicas; EspañaFil: Blanco Touriñán, Noel. Universidad Politécnica de Valencia; EspañaFil: Iserte, Javier Alonso. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Calleja Cabrera, Julián. Universidad Politécnica de Valencia; EspañaFil: Perea Resa, Carlos. Consejo Superior de Investigaciones Científicas; EspañaFil: Úrbez, Cristina. Universidad Politécnica de Valencia; EspañaFil: Carrasco, Pedro. Universidad Politécnica de Valencia; EspañaFil: Yanovsky, Marcelo Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Blázquez, Miguel A.. Universidad Politécnica de Valencia; EspañaFil: Salinas, Julio. Consejo Superior de Investigaciones Científicas; EspañaFil: Alabadí, David. Universidad Politécnica de Valencia; EspañaOxford University Press2020-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/138711Esteve Bruna, David; Carrasco López, Cristian; Blanco Touriñán, Noel; Iserte, Javier Alonso; Calleja Cabrera, Julián; et al.; Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis; Oxford University Press; Nucleic Acids Research; 48; 11; 6-2020; 6280-62930305-10481362-4962CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/article/48/11/6280/5836189info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkaa354info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:54:13Zoai:ri.conicet.gov.ar:11336/138711instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:54:13.676CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
title Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
spellingShingle Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
Esteve Bruna, David
LSM2-8 complex
prefoldins
spliceosome
title_short Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
title_full Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
title_fullStr Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
title_full_unstemmed Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
title_sort Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis
dc.creator.none.fl_str_mv Esteve Bruna, David
Carrasco López, Cristian
Blanco Touriñán, Noel
Iserte, Javier Alonso
Calleja Cabrera, Julián
Perea Resa, Carlos
Úrbez, Cristina
Carrasco, Pedro
Yanovsky, Marcelo Javier
Blázquez, Miguel A.
Salinas, Julio
Alabadí, David
author Esteve Bruna, David
author_facet Esteve Bruna, David
Carrasco López, Cristian
Blanco Touriñán, Noel
Iserte, Javier Alonso
Calleja Cabrera, Julián
Perea Resa, Carlos
Úrbez, Cristina
Carrasco, Pedro
Yanovsky, Marcelo Javier
Blázquez, Miguel A.
Salinas, Julio
Alabadí, David
author_role author
author2 Carrasco López, Cristian
Blanco Touriñán, Noel
Iserte, Javier Alonso
Calleja Cabrera, Julián
Perea Resa, Carlos
Úrbez, Cristina
Carrasco, Pedro
Yanovsky, Marcelo Javier
Blázquez, Miguel A.
Salinas, Julio
Alabadí, David
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv LSM2-8 complex
prefoldins
spliceosome
topic LSM2-8 complex
prefoldins
spliceosome
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Although originally identified as the components of the complex aiding the cytosolic chaperonin CCT in the folding of actins and tubulins in the cytosol, prefoldins (PFDs) are emerging as novel regulators influencing gene expression in the nucleus. Work conducted mainly in yeast and animals showed that PFDs act as transcriptional regulators and participate in the nuclear proteostasis. To investigate new functions of PFDs, we performed a co-expression analysis in Arabidopsis thaliana. Results revealed co-expression between PFD and the Sm-like (LSM) genes, which encode the LSM2–8 spliceosome core complex, in this model organism. Here, we show that PFDs interact with and are required to maintain adequate levels of the LSM2–8 complex. Our data indicate that levels of the LSM8 protein, which defines and confers the functional specificity of the complex, are reduced in pfd mutants and in response to the Hsp90 inhibitor geldanamycin. We provide biochemical evidence showing that LSM8 is a client of Hsp90 and that PFD4 mediates the interaction between both proteins. Consistent with our results and with the role of the LSM2–8 complex in splicing through the stabilization of the U6 snRNA, pfd mutants showed reduced levels of this snRNA and altered pre-mRNA splicing patterns.
Fil: Esteve Bruna, David. Universidad Politécnica de Valencia; España
Fil: Carrasco López, Cristian. Consejo Superior de Investigaciones Científicas; España
Fil: Blanco Touriñán, Noel. Universidad Politécnica de Valencia; España
Fil: Iserte, Javier Alonso. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Calleja Cabrera, Julián. Universidad Politécnica de Valencia; España
Fil: Perea Resa, Carlos. Consejo Superior de Investigaciones Científicas; España
Fil: Úrbez, Cristina. Universidad Politécnica de Valencia; España
Fil: Carrasco, Pedro. Universidad Politécnica de Valencia; España
Fil: Yanovsky, Marcelo Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Blázquez, Miguel A.. Universidad Politécnica de Valencia; España
Fil: Salinas, Julio. Consejo Superior de Investigaciones Científicas; España
Fil: Alabadí, David. Universidad Politécnica de Valencia; España
description Although originally identified as the components of the complex aiding the cytosolic chaperonin CCT in the folding of actins and tubulins in the cytosol, prefoldins (PFDs) are emerging as novel regulators influencing gene expression in the nucleus. Work conducted mainly in yeast and animals showed that PFDs act as transcriptional regulators and participate in the nuclear proteostasis. To investigate new functions of PFDs, we performed a co-expression analysis in Arabidopsis thaliana. Results revealed co-expression between PFD and the Sm-like (LSM) genes, which encode the LSM2–8 spliceosome core complex, in this model organism. Here, we show that PFDs interact with and are required to maintain adequate levels of the LSM2–8 complex. Our data indicate that levels of the LSM8 protein, which defines and confers the functional specificity of the complex, are reduced in pfd mutants and in response to the Hsp90 inhibitor geldanamycin. We provide biochemical evidence showing that LSM8 is a client of Hsp90 and that PFD4 mediates the interaction between both proteins. Consistent with our results and with the role of the LSM2–8 complex in splicing through the stabilization of the U6 snRNA, pfd mutants showed reduced levels of this snRNA and altered pre-mRNA splicing patterns.
publishDate 2020
dc.date.none.fl_str_mv 2020-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/138711
Esteve Bruna, David; Carrasco López, Cristian; Blanco Touriñán, Noel; Iserte, Javier Alonso; Calleja Cabrera, Julián; et al.; Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis; Oxford University Press; Nucleic Acids Research; 48; 11; 6-2020; 6280-6293
0305-1048
1362-4962
CONICET Digital
CONICET
url http://hdl.handle.net/11336/138711
identifier_str_mv Esteve Bruna, David; Carrasco López, Cristian; Blanco Touriñán, Noel; Iserte, Javier Alonso; Calleja Cabrera, Julián; et al.; Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis; Oxford University Press; Nucleic Acids Research; 48; 11; 6-2020; 6280-6293
0305-1048
1362-4962
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/article/48/11/6280/5836189
info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkaa354
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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