Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE

10 p.-6 fig.

Detalhes bibliográficos
Autores: Melero, Roberto, Moro, Fernando, Pérez-Calvo, María Ángeles, Perales-Calvo, Judit, Quintana-Gallardo, Lucía, Llorca, Óscar, Muga, Arturo, Valpuesta, José M.
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/154158
Acesso em linha:http://hdl.handle.net/10261/154158
Access Level:acceso abierto
Palavra-chave:70-Kilodalton heat shock protein (Hsp70)
Chaperone
Chaperone DnaK (DnaK)
Electron microscopy (EM)
GrpE
Nucleotide exchange factor
Protein folding
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repository_id_str
spelling Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpEMelero, RobertoMoro, FernandoPérez-Calvo, María ÁngelesPerales-Calvo, JuditQuintana-Gallardo, LucíaLlorca, ÓscarMuga, ArturoValpuesta, José M.70-Kilodalton heat shock protein (Hsp70)ChaperoneChaperone DnaK (DnaK)Electron microscopy (EM)GrpENucleotide exchange factorProtein folding10 p.-6 fig.Hsp70 chaperones comprise two domains, the nucleotide-binding domain (Hsp70NBD), responsible for structural and functional changes in the chaperone, and the substrate-binding domain (Hsp70SBD), involved in substrate interaction. Substrate binding and release in Hsp70 is controlled by the nucleotide state of DnaKNBD, with ATP inducing the open, substrate-receptive DnaKSBD conformation, whereas ADP forces its closure. DnaK cycles between the two conformations through interaction with two cofactors, the Hsp40 co-chaperones (DnaJ in Escherichia coli) induce the ADP state, and the nucleotide exchange factors (GrpE in E. coli) induce the ATP state. X-ray crystallography showed that the GrpE dimer is a nucleotide exchange factor that works by interaction of one of its monomers with DnaKNBD. DnaKSBD location in this complex is debated; there is evidence that it interacts with the GrpE N-terminal disordered region, far from DnaKNBD. Although we confirmed this interaction using biochemical and biophysical techniques, our EM-based three-dimensional reconstruction of the DnaK-GrpE complex located DnaKSBD near DnaKNBD. This apparent discrepancy between the functional and structural results is explained by our finding that the tail region of the GrpE dimer in the DnaK-GrpE complex bends and its tip contacts DnaKSBD, whereas the DnaKNBD-DnaKSBD linker contacts the GrpE helical region. We suggest that these interactions define a more complex role for GrpE in the control of DnaK function.This work was supported in part by Spanish Ministry of Economy and Innovation Grants BFU2013-44202 (to J. M. V.), SAF2011-22988 (to O. L.), and BFU2013-47059 (to A. M.), Madrid Regional Government Grants S2013/MIT-2807 (to J. M. V.) and S2010/BMD-2316 (to O. L.), and Basque Government Grant IT709-13 (to A. M.).Peer reviewedAmerican Society for Biochemistry and Molecular BiologyMinisterio de Ciencia e Innovación (España)Comunidad de MadridEusko JaurlaritzaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201720172015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/154158reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2013-44202-Pinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2013-47059-Phttp://dx.doi.org/10.1074/jbc.M114.623371Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1541582026-05-22T06:33:51Z
dc.title.none.fl_str_mv Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
title Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
spellingShingle Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
Melero, Roberto
70-Kilodalton heat shock protein (Hsp70)
Chaperone
Chaperone DnaK (DnaK)
Electron microscopy (EM)
GrpE
Nucleotide exchange factor
Protein folding
title_short Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
title_full Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
title_fullStr Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
title_full_unstemmed Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
title_sort Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
dc.creator.none.fl_str_mv Melero, Roberto
Moro, Fernando
Pérez-Calvo, María Ángeles
Perales-Calvo, Judit
Quintana-Gallardo, Lucía
Llorca, Óscar
Muga, Arturo
Valpuesta, José M.
author Melero, Roberto
author_facet Melero, Roberto
Moro, Fernando
Pérez-Calvo, María Ángeles
Perales-Calvo, Judit
Quintana-Gallardo, Lucía
Llorca, Óscar
Muga, Arturo
Valpuesta, José M.
author_role author
author2 Moro, Fernando
Pérez-Calvo, María Ángeles
Perales-Calvo, Judit
Quintana-Gallardo, Lucía
Llorca, Óscar
Muga, Arturo
Valpuesta, José M.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
Comunidad de Madrid
Eusko Jaurlaritza
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv 70-Kilodalton heat shock protein (Hsp70)
Chaperone
Chaperone DnaK (DnaK)
Electron microscopy (EM)
GrpE
Nucleotide exchange factor
Protein folding
topic 70-Kilodalton heat shock protein (Hsp70)
Chaperone
Chaperone DnaK (DnaK)
Electron microscopy (EM)
GrpE
Nucleotide exchange factor
Protein folding
description 10 p.-6 fig.
publishDate 2015
dc.date.none.fl_str_mv 2015
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/154158
url http://hdl.handle.net/10261/154158
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2013-44202-P
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2013-47059-P
http://dx.doi.org/10.1074/jbc.M114.623371
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869422277370576896
score 15.198674

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