The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins

Autores
Gómez Mínguez, Yaiza; Palacios Abella, Alberto; Costigliolo Rojas, María Cecilia; Barber, Mariana; Hernández Villa, Laura; Úrbez, Cristina; Alabadí, David
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The prefoldin-like protein UNCONVENTIONAL PREFOLDIN RPB5INTERACTOR (URI) participates in diverse cellular functions, includingprotein homeostasis, transcription, translation, and signal transduction. Thus,URI is a highly versatile protein, although the molecular basis of this versatil-ity remains unknown. In this work, we show that Arabidopsis thaliana(Arabidopsis) URI (AtURI) possesses a large intrinsically disordered region(IDR) spanning most of the C-terminal part of the protein, a feature con-served in yeast and human orthologs. Our findings reveal two key characteris-tics of disordered proteins in AtURI: promiscuity in interacting with partnersand protein instability. We propose that these two features contribute to pro-viding AtURI with functional versatility.
Fil: Gómez Mínguez, Yaiza. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Palacios Abella, Alberto. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Costigliolo Rojas, María Cecilia. 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. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Barber, Mariana. 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: Hernández Villa, Laura. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Úrbez, Cristina. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Alabadí, David. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Materia
INTERACTOME
PROTEIN DISORDER
PROTEIN STABILITY
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:11336/261735
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteinsGómez Mínguez, YaizaPalacios Abella, AlbertoCostigliolo Rojas, María CeciliaBarber, MarianaHernández Villa, LauraÚrbez, CristinaAlabadí, DavidINTERACTOMEPROTEIN DISORDERPROTEIN STABILITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The prefoldin-like protein UNCONVENTIONAL PREFOLDIN RPB5INTERACTOR (URI) participates in diverse cellular functions, includingprotein homeostasis, transcription, translation, and signal transduction. Thus,URI is a highly versatile protein, although the molecular basis of this versatil-ity remains unknown. In this work, we show that Arabidopsis thaliana(Arabidopsis) URI (AtURI) possesses a large intrinsically disordered region(IDR) spanning most of the C-terminal part of the protein, a feature con-served in yeast and human orthologs. Our findings reveal two key characteris-tics of disordered proteins in AtURI: promiscuity in interacting with partnersand protein instability. We propose that these two features contribute to pro-viding AtURI with functional versatility.Fil: Gómez Mínguez, Yaiza. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;Fil: Palacios Abella, Alberto. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;Fil: Costigliolo Rojas, María Cecilia. 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. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;Fil: Barber, Mariana. 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: Hernández Villa, Laura. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;Fil: Úrbez, Cristina. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;Fil: Alabadí, David. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;Wiley2024-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/261735Gómez Mínguez, Yaiza; Palacios Abella, Alberto; Costigliolo Rojas, María Cecilia; Barber, Mariana; Hernández Villa, Laura; et al.; The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins; Wiley; FEBS Letters; 598; 5; 2-2024; 556-5700014-5793CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14811info:eu-repo/semantics/altIdentifier/doi/10.1002/1873-3468.14811info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:46:24Zoai:ri.conicet.gov.ar:11336/261735instacron: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:34982025-09-03 09:46:24.755CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
title The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
spellingShingle The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
Gómez Mínguez, Yaiza
INTERACTOME
PROTEIN DISORDER
PROTEIN STABILITY
title_short The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
title_full The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
title_fullStr The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
title_full_unstemmed The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
title_sort The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
dc.creator.none.fl_str_mv Gómez Mínguez, Yaiza
Palacios Abella, Alberto
Costigliolo Rojas, María Cecilia
Barber, Mariana
Hernández Villa, Laura
Úrbez, Cristina
Alabadí, David
author Gómez Mínguez, Yaiza
author_facet Gómez Mínguez, Yaiza
Palacios Abella, Alberto
Costigliolo Rojas, María Cecilia
Barber, Mariana
Hernández Villa, Laura
Úrbez, Cristina
Alabadí, David
author_role author
author2 Palacios Abella, Alberto
Costigliolo Rojas, María Cecilia
Barber, Mariana
Hernández Villa, Laura
Úrbez, Cristina
Alabadí, David
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv INTERACTOME
PROTEIN DISORDER
PROTEIN STABILITY
topic INTERACTOME
PROTEIN DISORDER
PROTEIN STABILITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The prefoldin-like protein UNCONVENTIONAL PREFOLDIN RPB5INTERACTOR (URI) participates in diverse cellular functions, includingprotein homeostasis, transcription, translation, and signal transduction. Thus,URI is a highly versatile protein, although the molecular basis of this versatil-ity remains unknown. In this work, we show that Arabidopsis thaliana(Arabidopsis) URI (AtURI) possesses a large intrinsically disordered region(IDR) spanning most of the C-terminal part of the protein, a feature con-served in yeast and human orthologs. Our findings reveal two key characteris-tics of disordered proteins in AtURI: promiscuity in interacting with partnersand protein instability. We propose that these two features contribute to pro-viding AtURI with functional versatility.
Fil: Gómez Mínguez, Yaiza. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Palacios Abella, Alberto. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Costigliolo Rojas, María Cecilia. 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. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Barber, Mariana. 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: Hernández Villa, Laura. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Úrbez, Cristina. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
Fil: Alabadí, David. Instituto de Biología Molecular y Celular de Plantas ; Universidad Politecnica de Valencia;
description The prefoldin-like protein UNCONVENTIONAL PREFOLDIN RPB5INTERACTOR (URI) participates in diverse cellular functions, includingprotein homeostasis, transcription, translation, and signal transduction. Thus,URI is a highly versatile protein, although the molecular basis of this versatil-ity remains unknown. In this work, we show that Arabidopsis thaliana(Arabidopsis) URI (AtURI) possesses a large intrinsically disordered region(IDR) spanning most of the C-terminal part of the protein, a feature con-served in yeast and human orthologs. Our findings reveal two key characteris-tics of disordered proteins in AtURI: promiscuity in interacting with partnersand protein instability. We propose that these two features contribute to pro-viding AtURI with functional versatility.
publishDate 2024
dc.date.none.fl_str_mv 2024-02
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/11336/261735
Gómez Mínguez, Yaiza; Palacios Abella, Alberto; Costigliolo Rojas, María Cecilia; Barber, Mariana; Hernández Villa, Laura; et al.; The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins; Wiley; FEBS Letters; 598; 5; 2-2024; 556-570
0014-5793
CONICET Digital
CONICET
url http://hdl.handle.net/11336/261735
identifier_str_mv Gómez Mínguez, Yaiza; Palacios Abella, Alberto; Costigliolo Rojas, María Cecilia; Barber, Mariana; Hernández Villa, Laura; et al.; The prefoldin‐like protein AtURI exhibits characteristics of intrinsically disordered proteins; Wiley; FEBS Letters; 598; 5; 2-2024; 556-570
0014-5793
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://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14811
info:eu-repo/semantics/altIdentifier/doi/10.1002/1873-3468.14811
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
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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score 13.13397

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