The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system

13 p.-4 fig.-1 tab.

Detalles Bibliográficos
Autores: Rivera-Calzada, Angel, Pal, Mohinder, Luque-Ortega, Juan Román, Gil-Cartón, David, Degliesposti, Gianluca, Skehel, J. Mark, Prodromou, Chrisostomos, Pearl, Laurence H., Llorca, Óscar
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/154080
Acceso en línea:http://hdl.handle.net/10261/154080
Access Level:acceso abierto
Palabra clave:Tah1
Rvb1
Rvb2
Hsp90 co-chaperone
Pih1
R2TP complex
Tel2-Tti1-Tti2
Cryo-electron microscopy (cryo-EM)
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repository_id_str
spelling The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone systemRivera-Calzada, AngelPal, MohinderLuque-Ortega, Juan RománGil-Cartón, DavidDegliesposti, GianlucaSkehel, J. MarkProdromou, ChrisostomosPearl, Laurence H.Llorca, ÓscarTah1Rvb1Rvb2Hsp90 co-chaperonePih1R2TP complexTel2-Tti1-Tti2Cryo-electron microscopy (cryo-EM)13 p.-4 fig.-1 tab.The R2TP complex, comprising the Rvb1p-Rvb2p AAA-ATPases, Tah1p, and Pih1p in yeast, is a specialized Hsp90 co-chaperone required for the assembly and maturation of multi-subunit complexes. These include the small nucleolar ribonucleoproteins, RNA polymerase II, and complexes containing phosphatidylinositol-3-kinase-like kinases. The structure and stoichiometry of yeast R2TP and how it couples to Hsp90 are currently unknown. Here, we determine the 3D organization of yeast R2TP using sedimentation velocity analysis and cryo-electron microscopy. The 359-kDa complex comprises one Rvb1p/Rvb2p hetero-hexamer with domains II (DIIs) forming an open basket that accommodates a single copy of Tah1p-Pih1p. Tah1p-Pih1p binding to multiple DII domains regulates Rvb1p/Rvb2p ATPase activity. Using domain dissection and cross-linking mass spectrometry, we identified a unique region of Pih1p that is essential for interaction with Rvb1p/Rvb2p. These data provide a structural basis for understanding how R2TP couples an Hsp90 dimer to a diverse set of client proteins and complexes.This work was supported by the Spanish Ministry of Economy, Industry and Competitiveness (SAF2014-52301-R to O.L.), the Spanish National Research Council (i-LINK0997 to O.L.), a Wellcome Trust Senior Investigator award (095605/Z/11/Z) and Award Enhancement Grant (095605/Z/11/A) (to L.H.P.). CESGA and the Supercomputing and Bioinnovation Center of the University of Malaga provided computational resources. The CIISB research infrastructure project LM2015043 funded by MEYS CR is acknowledged for the financial support of the measurements at the CF Cryo-electron Microscopy and Tomography CEITEC MU, as well as the help from Jiří Nováček. We are grateful for access to and support from the cryo-EM facilities at the UK National Electron Bio-imaging Center (eBIC), proposal EM14507, funded by the Wellcome Trust, MRC and BBSRC, and help of Dr. Daniel Clare. This work used the platforms of the Grenoble Instruct Center (ISBG: UMS 3518 CNRS-CEA-UJF-EMBL) and we were helped by Guy Schoehn (IBS-Grenoble). We thank Andrés Lopez-Perrote for his help.Peer reviewedElsevierMinisterio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201720172017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/154080reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2014-52301-Rhttps://doi.org/10.1016/j.str.2017.05.016Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1540802026-05-22T06:33:51Z
dc.title.none.fl_str_mv The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
title The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
spellingShingle The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
Rivera-Calzada, Angel
Tah1
Rvb1
Rvb2
Hsp90 co-chaperone
Pih1
R2TP complex
Tel2-Tti1-Tti2
Cryo-electron microscopy (cryo-EM)
title_short The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
title_full The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
title_fullStr The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
title_full_unstemmed The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
title_sort The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system
dc.creator.none.fl_str_mv Rivera-Calzada, Angel
Pal, Mohinder
Luque-Ortega, Juan Román
Gil-Cartón, David
Degliesposti, Gianluca
Skehel, J. Mark
Prodromou, Chrisostomos
Pearl, Laurence H.
Llorca, Óscar
author Rivera-Calzada, Angel
author_facet Rivera-Calzada, Angel
Pal, Mohinder
Luque-Ortega, Juan Román
Gil-Cartón, David
Degliesposti, Gianluca
Skehel, J. Mark
Prodromou, Chrisostomos
Pearl, Laurence H.
Llorca, Óscar
author_role author
author2 Pal, Mohinder
Luque-Ortega, Juan Román
Gil-Cartón, David
Degliesposti, Gianluca
Skehel, J. Mark
Prodromou, Chrisostomos
Pearl, Laurence H.
Llorca, Óscar
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Tah1
Rvb1
Rvb2
Hsp90 co-chaperone
Pih1
R2TP complex
Tel2-Tti1-Tti2
Cryo-electron microscopy (cryo-EM)
topic Tah1
Rvb1
Rvb2
Hsp90 co-chaperone
Pih1
R2TP complex
Tel2-Tti1-Tti2
Cryo-electron microscopy (cryo-EM)
description 13 p.-4 fig.-1 tab.
publishDate 2017
dc.date.none.fl_str_mv 2017
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/10261/154080
url http://hdl.handle.net/10261/154080
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2014-52301-R
https://doi.org/10.1016/j.str.2017.05.016
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
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score 15,811543

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