Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer

10 pages, 6 figures.-- PMID: 17517766 [PubMed].-- PMCID: PMC1920261.

Detalles Bibliográficos
Autores: Torreira, Eva, Schoehn, Guy, Fernández, Yolanda, Jorba, Núria, Ruigrok, Rob W. H., Cusack, Stephen, Ortín, Juan, Llorca, Óscar
Tipo de recurso: artículo
Fecha de publicación:2007
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/9455
Acceso en línea:http://hdl.handle.net/10261/9455
Access Level:acceso abierto
Palabra clave:Influenza A virus
Ribonucleoprotein complexes (RNPs)
RNA polymerase complex
Heterotrimer
Structural model
Conformational changes
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spelling Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimerTorreira, EvaSchoehn, GuyFernández, YolandaJorba, NúriaRuigrok, Rob W. H.Cusack, StephenOrtín, JuanLlorca, ÓscarInfluenza A virusRibonucleoprotein complexes (RNPs)RNA polymerase complexHeterotrimerStructural modelConformational changes10 pages, 6 figures.-- PMID: 17517766 [PubMed].-- PMCID: PMC1920261.The genome of influenza A virus is organized into eight ribonucleoprotein complexes (RNPs), each containing one RNA polymerase complex. This RNA polymerase has also been found non-associated to RNPs and is possibly involved in distinct functions in the infection cycle. We have expressed the virus RNA polymerase complex by co-tranfection of the PB1, PB2 and PA genes in mammalian cells and the heterotrimer was purified by the TAP tag procedure. Its 3D structure was determined by electron microscopy and single-particle image processing. The model obtained resembles the structure previously reported for the polymerase complex associated to viral RNPs but appears to be in a more open conformation. Detailed model comparison indicated that specific areas of the complex show important conformational changes as compared to the structure for the RNP-associated polymerase, particularly in regions known to interact with the adjacent NP monomers in the RNP. Also, the PB2 subunit seems to undergo a substantial displacement as a result of the association of the polymerase to RNPs. The structural model presented suggests that a core conformation of the polymerase in solution exists but the interaction with other partners, such as proteins or RNA, will trigger distinct conformational changes to activate new functional properties.This work was supported by the Spanish Ministry of Education and Science (Ministerio de Educación y Ciencia) (grants BMC2001-1223 and BFU2004-491 to JO and SAF2005-00775 and GEN2003-20239-C06-06 to OLL), the European Vigilance Network for the Management of Antiviral Drug Resistance (VIRGIL) and the FLUPOL strep project (SP5B-CT-2007-044263). Funding to pay the Open Access publication charges for this article was provided by Grant BFU2004-00491.Peer reviewedOxford University Press200920092007info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501574418 bytesapplication/pdfhttp://hdl.handle.net/10261/9455reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1093/nar/gkm336info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/94552026-05-22T06:33:51Z
dc.title.none.fl_str_mv Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
title Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
spellingShingle Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
Torreira, Eva
Influenza A virus
Ribonucleoprotein complexes (RNPs)
RNA polymerase complex
Heterotrimer
Structural model
Conformational changes
title_short Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
title_full Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
title_fullStr Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
title_full_unstemmed Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
title_sort Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
dc.creator.none.fl_str_mv Torreira, Eva
Schoehn, Guy
Fernández, Yolanda
Jorba, Núria
Ruigrok, Rob W. H.
Cusack, Stephen
Ortín, Juan
Llorca, Óscar
author Torreira, Eva
author_facet Torreira, Eva
Schoehn, Guy
Fernández, Yolanda
Jorba, Núria
Ruigrok, Rob W. H.
Cusack, Stephen
Ortín, Juan
Llorca, Óscar
author_role author
author2 Schoehn, Guy
Fernández, Yolanda
Jorba, Núria
Ruigrok, Rob W. H.
Cusack, Stephen
Ortín, Juan
Llorca, Óscar
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Influenza A virus
Ribonucleoprotein complexes (RNPs)
RNA polymerase complex
Heterotrimer
Structural model
Conformational changes
topic Influenza A virus
Ribonucleoprotein complexes (RNPs)
RNA polymerase complex
Heterotrimer
Structural model
Conformational changes
description 10 pages, 6 figures.-- PMID: 17517766 [PubMed].-- PMCID: PMC1920261.
publishDate 2007
dc.date.none.fl_str_mv 2007
2009
2009
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/9455
url http://hdl.handle.net/10261/9455
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/gkm336
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 574418 bytes
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: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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