Dimerization model of the C-terminal RNA Recognition Motif of HuR

Human antigen R (HuR) is a ubiquitous 32kDa protein comprising three RNA Recognition Motifs (RRMs), whose main function is to bind Adenylate and uridylate Rich Elements (AREs) in 3′ UnTranslated Regions (UTRs) of mRNAs. In addition to binding RNA molecules, the third domain (RRM3) is involved in HuR...

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Autores: Díaz Quintana, Antonio Jesús, García Mauriño, Sofía M., Díaz Moreno, Irene
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2015
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/69174
Acceso en línea:https://hdl.handle.net/11441/69174
https://doi.org/10.1016/j.febslet.2015.03.013
Access Level:acceso abierto
Palabra clave:Dimerization
Human antigen R (HuR)
RNA Binding Protein
RNA Recognition Motif (RRM)
Brownian Dynamics (BD)
Molecular Dynamics (MD)
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spelling Dimerization model of the C-terminal RNA Recognition Motif of HuRDíaz Quintana, Antonio JesúsGarcía Mauriño, Sofía M.Díaz Moreno, IreneDimerizationHuman antigen R (HuR)RNA Binding ProteinRNA Recognition Motif (RRM)Brownian Dynamics (BD)Molecular Dynamics (MD)Human antigen R (HuR) is a ubiquitous 32kDa protein comprising three RNA Recognition Motifs (RRMs), whose main function is to bind Adenylate and uridylate Rich Elements (AREs) in 3′ UnTranslated Regions (UTRs) of mRNAs. In addition to binding RNA molecules, the third domain (RRM3) is involved in HuR oligomerization and apoptotic signaling. The RRM3 monomer is able to dimerize, with its self-binding affinity being dependent on ionic strength. Here we provide a deeper structural insight into the nature of the encounter complexes leading to the formation of RRM3 dimers by using Brownian Dynamics and Molecular Dynamics. Our computational data show that the initial unspecific encounter follows a downhill pathway until reaching an optimum conformation stabilized by hydrophobic interactions.Junta de Andalucía P07-CVI-02896, P11-CVI-07216 and 290 BIO198wileyBioquímica Vegetal y Biología MolecularJunta de Andalucía2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/69174https://doi.org/10.1016/j.febslet.2015.03.013reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésFEBS Letters, 589 (10), 1059-1066.P07-CVI-02896P11-CVI-07216290 BIO198http://dx.doi.org/10.1016/j.febslet.2015.03.013info:eu-repo/semantics/openAccessoai:idus.us.es:11441/691742026-06-17T12:51:07Z
dc.title.none.fl_str_mv Dimerization model of the C-terminal RNA Recognition Motif of HuR
title Dimerization model of the C-terminal RNA Recognition Motif of HuR
spellingShingle Dimerization model of the C-terminal RNA Recognition Motif of HuR
Díaz Quintana, Antonio Jesús
Dimerization
Human antigen R (HuR)
RNA Binding Protein
RNA Recognition Motif (RRM)
Brownian Dynamics (BD)
Molecular Dynamics (MD)
title_short Dimerization model of the C-terminal RNA Recognition Motif of HuR
title_full Dimerization model of the C-terminal RNA Recognition Motif of HuR
title_fullStr Dimerization model of the C-terminal RNA Recognition Motif of HuR
title_full_unstemmed Dimerization model of the C-terminal RNA Recognition Motif of HuR
title_sort Dimerization model of the C-terminal RNA Recognition Motif of HuR
dc.creator.none.fl_str_mv Díaz Quintana, Antonio Jesús
García Mauriño, Sofía M.
Díaz Moreno, Irene
author Díaz Quintana, Antonio Jesús
author_facet Díaz Quintana, Antonio Jesús
García Mauriño, Sofía M.
Díaz Moreno, Irene
author_role author
author2 García Mauriño, Sofía M.
Díaz Moreno, Irene
author2_role author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Junta de Andalucía
dc.subject.none.fl_str_mv Dimerization
Human antigen R (HuR)
RNA Binding Protein
RNA Recognition Motif (RRM)
Brownian Dynamics (BD)
Molecular Dynamics (MD)
topic Dimerization
Human antigen R (HuR)
RNA Binding Protein
RNA Recognition Motif (RRM)
Brownian Dynamics (BD)
Molecular Dynamics (MD)
description Human antigen R (HuR) is a ubiquitous 32kDa protein comprising three RNA Recognition Motifs (RRMs), whose main function is to bind Adenylate and uridylate Rich Elements (AREs) in 3′ UnTranslated Regions (UTRs) of mRNAs. In addition to binding RNA molecules, the third domain (RRM3) is involved in HuR oligomerization and apoptotic signaling. The RRM3 monomer is able to dimerize, with its self-binding affinity being dependent on ionic strength. Here we provide a deeper structural insight into the nature of the encounter complexes leading to the formation of RRM3 dimers by using Brownian Dynamics and Molecular Dynamics. Our computational data show that the initial unspecific encounter follows a downhill pathway until reaching an optimum conformation stabilized by hydrophobic interactions.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/69174
https://doi.org/10.1016/j.febslet.2015.03.013
url https://hdl.handle.net/11441/69174
https://doi.org/10.1016/j.febslet.2015.03.013
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv FEBS Letters, 589 (10), 1059-1066.
P07-CVI-02896
P11-CVI-07216
290 BIO198
http://dx.doi.org/10.1016/j.febslet.2015.03.013
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 wiley
publisher.none.fl_str_mv wiley
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 15,301603

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