Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex

RuvBL1 and RuvBL2, also known as Pontin and Reptin, are AAA+ proteins essential in small nucleolar ribonucloprotein biogenesis, chromatin remodelling, nonsense-mediated messenger RNA decay and telomerase assembly, among other functions.They are homologous to prokaryotic RuvB, forming single- and dou...

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Detalles Bibliográficos
Autores: López-Perrote, Andrés, Muñoz-Hernández, Hugo, Gil, David, Llorca, Óscar
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2012
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/96345
Acceso en línea:http://hdl.handle.net/10261/96345
Access Level:acceso abierto
Palabra clave:RuvBL1
RuvBL2
Rvb1
Rvb2
AAA+ ATPases
Electron microscopy
Chromatin remodeling
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spelling Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complexLópez-Perrote, AndrésMuñoz-Hernández, HugoGil, DavidLlorca, ÓscarRuvBL1RuvBL2Rvb1Rvb2AAA+ ATPasesElectron microscopyChromatin remodelingRuvBL1 and RuvBL2, also known as Pontin and Reptin, are AAA+ proteins essential in small nucleolar ribonucloprotein biogenesis, chromatin remodelling, nonsense-mediated messenger RNA decay and telomerase assembly, among other functions.They are homologous to prokaryotic RuvB, forming single- and double-hexameric rings; however, a DNA binding domain II (DII) is inserted within the AAA+ core. Despite their biological significance, questions remain regarding their structure. Here, we report cryo-electron microscopy structures of human double-ring RuvBL1–RuvBL2 complexes at 15A ° resolution. Significantly, we resolve two coexisting conformations, compact and stretched, by image classification techniques. Movements in DII domains drive these conformational transitions, extending the complex and regulating the exposure of DNA binding regions. DII domains connect with the AAA+core and bind nucleic acids, suggesting that these conformational changes could impact the regulation of RuvBL1–RuvBL2 containing complexes. These findings resolve some of the controversies in the structure of RuvBL1–RuvBL2 by revealing a mechanism that extends the complex by adjustments in DIISpanish Government [SAF2008-00451 to O.L., SAF2011-22988 to O.L.]; [BES-2009-014133 to A.L-P.]; ‘Red Temática de Investigación Cooperativa en Cáncer(RTICC)’ [RD06/0020/1001]; Human Frontiers Science Program [RGP39/2008]‘Ramón Areces’Foundation.Funding for open access charge: Spanish Government [SAF2011-22988 to O.L.].Peer reviewedOxford University Press201420142012info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/96345reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1093/nar/gks871info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/963452026-05-22T06:33:51Z
dc.title.none.fl_str_mv Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
title Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
spellingShingle Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
López-Perrote, Andrés
RuvBL1
RuvBL2
Rvb1
Rvb2
AAA+ ATPases
Electron microscopy
Chromatin remodeling
title_short Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
title_full Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
title_fullStr Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
title_full_unstemmed Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
title_sort Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
dc.creator.none.fl_str_mv López-Perrote, Andrés
Muñoz-Hernández, Hugo
Gil, David
Llorca, Óscar
author López-Perrote, Andrés
author_facet López-Perrote, Andrés
Muñoz-Hernández, Hugo
Gil, David
Llorca, Óscar
author_role author
author2 Muñoz-Hernández, Hugo
Gil, David
Llorca, Óscar
author2_role author
author
author
dc.subject.none.fl_str_mv RuvBL1
RuvBL2
Rvb1
Rvb2
AAA+ ATPases
Electron microscopy
Chromatin remodeling
topic RuvBL1
RuvBL2
Rvb1
Rvb2
AAA+ ATPases
Electron microscopy
Chromatin remodeling
description RuvBL1 and RuvBL2, also known as Pontin and Reptin, are AAA+ proteins essential in small nucleolar ribonucloprotein biogenesis, chromatin remodelling, nonsense-mediated messenger RNA decay and telomerase assembly, among other functions.They are homologous to prokaryotic RuvB, forming single- and double-hexameric rings; however, a DNA binding domain II (DII) is inserted within the AAA+ core. Despite their biological significance, questions remain regarding their structure. Here, we report cryo-electron microscopy structures of human double-ring RuvBL1–RuvBL2 complexes at 15A ° resolution. Significantly, we resolve two coexisting conformations, compact and stretched, by image classification techniques. Movements in DII domains drive these conformational transitions, extending the complex and regulating the exposure of DNA binding regions. DII domains connect with the AAA+core and bind nucleic acids, suggesting that these conformational changes could impact the regulation of RuvBL1–RuvBL2 containing complexes. These findings resolve some of the controversies in the structure of RuvBL1–RuvBL2 by revealing a mechanism that extends the complex by adjustments in DII
publishDate 2012
dc.date.none.fl_str_mv 2012
2014
2014
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/10261/96345
url http://hdl.handle.net/10261/96345
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1093/nar/gks871
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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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