Induced folding in RNA recognition by Arabidopsis thaliana DCL1

Autores
Suarez, Irina Paula; Burdisso, Paula; Benoit Matthieu P. M. H.; Boisbouvier, Jerome; Rasia, Rodolfo Maximiliano
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
DCL1 is the ribonuclease that carries out miRNA biogenesis in plants. The enzyme has two tandem double stranded RNA binding domains (dsRBDs) in its C-terminus. Here we show that the first of these domains binds precursor RNA fragments when isolated and cooperates with the second domain in the recognition of substrate RNA. Remarkably, despite showing RNA binding activity, this domain is intrinsically disordered. We found that it acquires a folded conformation when bound to its substrate, being the first report of a complete dsRBD folding upon binding. The free unfolded form shows tendency to adopt folded conformations, and goes through an unfolded bound state prior to the folding event. The significance of these results is discussed by comparison with the behavior of other dsRBDs.
Fil: Suarez, Irina Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Burdisso, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Benoit Matthieu P. M. H.. Institut de Biologie Structurale Jean Pierre Ebel; Francia
Fil: Boisbouvier, Jerome. Institut de Biologie Structurale Jean Pierre Ebel; Francia
Fil: Rasia, Rodolfo Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
DCL1
miRNA
dsRBDs
INTRINSICALLY DISORDERED
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:11336/51106
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Induced folding in RNA recognition by Arabidopsis thaliana DCL1Suarez, Irina PaulaBurdisso, PaulaBenoit Matthieu P. M. H.Boisbouvier, JeromeRasia, Rodolfo MaximilianoDCL1miRNAdsRBDsINTRINSICALLY DISORDEREDhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1DCL1 is the ribonuclease that carries out miRNA biogenesis in plants. The enzyme has two tandem double stranded RNA binding domains (dsRBDs) in its C-terminus. Here we show that the first of these domains binds precursor RNA fragments when isolated and cooperates with the second domain in the recognition of substrate RNA. Remarkably, despite showing RNA binding activity, this domain is intrinsically disordered. We found that it acquires a folded conformation when bound to its substrate, being the first report of a complete dsRBD folding upon binding. The free unfolded form shows tendency to adopt folded conformations, and goes through an unfolded bound state prior to the folding event. The significance of these results is discussed by comparison with the behavior of other dsRBDs.Fil: Suarez, Irina Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Burdisso, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Benoit Matthieu P. M. H.. Institut de Biologie Structurale Jean Pierre Ebel; FranciaFil: Boisbouvier, Jerome. Institut de Biologie Structurale Jean Pierre Ebel; FranciaFil: Rasia, Rodolfo Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaOxford University Press2015-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/51106Suarez, Irina Paula; Burdisso, Paula; Benoit Matthieu P. M. H.; Boisbouvier, Jerome; Rasia, Rodolfo Maximiliano; Induced folding in RNA recognition by Arabidopsis thaliana DCL1; Oxford University Press; Nucleic Acids Research; 43; 13; 6-2015; 6607-66190305-10481362-4962CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkv627info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/article/43/13/6607/2414337info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:43:35Zoai:ri.conicet.gov.ar:11336/51106instacron: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 09:43:35.449CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Induced folding in RNA recognition by Arabidopsis thaliana DCL1
title Induced folding in RNA recognition by Arabidopsis thaliana DCL1
spellingShingle Induced folding in RNA recognition by Arabidopsis thaliana DCL1
Suarez, Irina Paula
DCL1
miRNA
dsRBDs
INTRINSICALLY DISORDERED
title_short Induced folding in RNA recognition by Arabidopsis thaliana DCL1
title_full Induced folding in RNA recognition by Arabidopsis thaliana DCL1
title_fullStr Induced folding in RNA recognition by Arabidopsis thaliana DCL1
title_full_unstemmed Induced folding in RNA recognition by Arabidopsis thaliana DCL1
title_sort Induced folding in RNA recognition by Arabidopsis thaliana DCL1
dc.creator.none.fl_str_mv Suarez, Irina Paula
Burdisso, Paula
Benoit Matthieu P. M. H.
Boisbouvier, Jerome
Rasia, Rodolfo Maximiliano
author Suarez, Irina Paula
author_facet Suarez, Irina Paula
Burdisso, Paula
Benoit Matthieu P. M. H.
Boisbouvier, Jerome
Rasia, Rodolfo Maximiliano
author_role author
author2 Burdisso, Paula
Benoit Matthieu P. M. H.
Boisbouvier, Jerome
Rasia, Rodolfo Maximiliano
author2_role author
author
author
author
dc.subject.none.fl_str_mv DCL1
miRNA
dsRBDs
INTRINSICALLY DISORDERED
topic DCL1
miRNA
dsRBDs
INTRINSICALLY DISORDERED
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv DCL1 is the ribonuclease that carries out miRNA biogenesis in plants. The enzyme has two tandem double stranded RNA binding domains (dsRBDs) in its C-terminus. Here we show that the first of these domains binds precursor RNA fragments when isolated and cooperates with the second domain in the recognition of substrate RNA. Remarkably, despite showing RNA binding activity, this domain is intrinsically disordered. We found that it acquires a folded conformation when bound to its substrate, being the first report of a complete dsRBD folding upon binding. The free unfolded form shows tendency to adopt folded conformations, and goes through an unfolded bound state prior to the folding event. The significance of these results is discussed by comparison with the behavior of other dsRBDs.
Fil: Suarez, Irina Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Burdisso, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Benoit Matthieu P. M. H.. Institut de Biologie Structurale Jean Pierre Ebel; Francia
Fil: Boisbouvier, Jerome. Institut de Biologie Structurale Jean Pierre Ebel; Francia
Fil: Rasia, Rodolfo Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description DCL1 is the ribonuclease that carries out miRNA biogenesis in plants. The enzyme has two tandem double stranded RNA binding domains (dsRBDs) in its C-terminus. Here we show that the first of these domains binds precursor RNA fragments when isolated and cooperates with the second domain in the recognition of substrate RNA. Remarkably, despite showing RNA binding activity, this domain is intrinsically disordered. We found that it acquires a folded conformation when bound to its substrate, being the first report of a complete dsRBD folding upon binding. The free unfolded form shows tendency to adopt folded conformations, and goes through an unfolded bound state prior to the folding event. The significance of these results is discussed by comparison with the behavior of other dsRBDs.
publishDate 2015
dc.date.none.fl_str_mv 2015-06
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/11336/51106
Suarez, Irina Paula; Burdisso, Paula; Benoit Matthieu P. M. H.; Boisbouvier, Jerome; Rasia, Rodolfo Maximiliano; Induced folding in RNA recognition by Arabidopsis thaliana DCL1; Oxford University Press; Nucleic Acids Research; 43; 13; 6-2015; 6607-6619
0305-1048
1362-4962
CONICET Digital
CONICET
url http://hdl.handle.net/11336/51106
identifier_str_mv Suarez, Irina Paula; Burdisso, Paula; Benoit Matthieu P. M. H.; Boisbouvier, Jerome; Rasia, Rodolfo Maximiliano; Induced folding in RNA recognition by Arabidopsis thaliana DCL1; Oxford University Press; Nucleic Acids Research; 43; 13; 6-2015; 6607-6619
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/doi/10.1093/nar/gkv627
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/article/43/13/6607/2414337
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
_version_ 1842268611901652992
score 13.13397

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