Human mitochondrial complex I assembly is mediated by NDUFAF1

24 p.-7 fig.

Detalles Bibliográficos
Autores: Vogel, Rutger, Janssen, Rolf J., Ugalde, Cristina, Grovenstein, Melissa, Huijbens, Richard, Visch, Henk-Jan, van den Heuvel, Lambert P., Willems, Peter H., Zeviani, Massimo, Smeitink, Jan A., Nijtmans, Leo G.
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2005
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/377957
Acceso en línea:http://hdl.handle.net/10261/377957
Access Level:acceso abierto
Palabra clave:Assembly
NDUFAF1
Complex I
Mitochondria
Oxidative phosphorylation
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spelling Human mitochondrial complex I assembly is mediated by NDUFAF1Running Title: NDUFAF1 mediates complex I assemblyVogel, RutgerJanssen, Rolf J.Ugalde, CristinaGrovenstein, MelissaHuijbens, RichardVisch, Henk-Janvan den Heuvel, Lambert P.Willems, Peter H.Zeviani, MassimoSmeitink, Jan A.Nijtmans, Leo G.AssemblyNDUFAF1Complex IMitochondriaOxidative phosphorylation24 p.-7 fig.Complex I (NADH:ubiquinone oxidoreductase) is the largest multiprotein enzyme of the oxidative phosphorylation system. Its assembly in human cells is poorly understood and no proteins assisting this process have yet been described. A good candidate is NDUFAF1, the human homologue of Neurospora crassa complex I chaperone CIA30. Here, we demonstrate that NDUFAF1 is a mitochondrial protein that is involved in the complex I assembly process. Modulating the intramitochondrial amount of NDUFAF1 by knocking down its expression using RNA interference leads to a reduced amount and activity of complex I. NDUFAF1 is associated to two complexes of 600 and 700 kDa in size of which the relative distribution is altered in two complex I deficient patients. Analysis of NDUFAF1 expression in a conditional complex I assembly system shows that the 700 kDa complex may represent a key step in the complex I assembly process. Based on these data, we propose that NDUFAF1 is an important protein for the assembly/stability of complex I.This work was supported by ‘Het Prinses Beatrix Fonds’ to J.S and B. vdH. (grant number 02–0104) and the European Community's sixth Framework Programme for Research, Priority 1 ‘Life sciences, genomics and biotechnology for health’ (contract number LSHMCT-2004–503116). The Netherlands Organization for Scientific Research supported L.N. with a ‘Vernieuwingsimpuls’ grant. CU is recipient of a research contract from Instituto de Salud Carlos III (ISC III CP04/00011).Peer reviewedJohn Wiley & SonsPrincess Beatrix Muscle FundEuropean CommissionNetherlands Organization for Scientific ResearchInstituto de Salud Carlos IIIUgalde, Cristina [0000-0002-9742-1877]Zeviani, Massimo [0000-0002-9067-5508]202520252005info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/377957reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1111/j.1742-4658.2005.04928.xNoinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3779572026-05-22T06:33:51Z
dc.title.none.fl_str_mv Human mitochondrial complex I assembly is mediated by NDUFAF1
Running Title: NDUFAF1 mediates complex I assembly
title Human mitochondrial complex I assembly is mediated by NDUFAF1
spellingShingle Human mitochondrial complex I assembly is mediated by NDUFAF1
Vogel, Rutger
Assembly
NDUFAF1
Complex I
Mitochondria
Oxidative phosphorylation
title_short Human mitochondrial complex I assembly is mediated by NDUFAF1
title_full Human mitochondrial complex I assembly is mediated by NDUFAF1
title_fullStr Human mitochondrial complex I assembly is mediated by NDUFAF1
title_full_unstemmed Human mitochondrial complex I assembly is mediated by NDUFAF1
title_sort Human mitochondrial complex I assembly is mediated by NDUFAF1
dc.creator.none.fl_str_mv Vogel, Rutger
Janssen, Rolf J.
Ugalde, Cristina
Grovenstein, Melissa
Huijbens, Richard
Visch, Henk-Jan
van den Heuvel, Lambert P.
Willems, Peter H.
Zeviani, Massimo
Smeitink, Jan A.
Nijtmans, Leo G.
author Vogel, Rutger
author_facet Vogel, Rutger
Janssen, Rolf J.
Ugalde, Cristina
Grovenstein, Melissa
Huijbens, Richard
Visch, Henk-Jan
van den Heuvel, Lambert P.
Willems, Peter H.
Zeviani, Massimo
Smeitink, Jan A.
Nijtmans, Leo G.
author_role author
author2 Janssen, Rolf J.
Ugalde, Cristina
Grovenstein, Melissa
Huijbens, Richard
Visch, Henk-Jan
van den Heuvel, Lambert P.
Willems, Peter H.
Zeviani, Massimo
Smeitink, Jan A.
Nijtmans, Leo G.
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Princess Beatrix Muscle Fund
European Commission
Netherlands Organization for Scientific Research
Instituto de Salud Carlos III
Ugalde, Cristina [0000-0002-9742-1877]
Zeviani, Massimo [0000-0002-9067-5508]
dc.subject.none.fl_str_mv Assembly
NDUFAF1
Complex I
Mitochondria
Oxidative phosphorylation
topic Assembly
NDUFAF1
Complex I
Mitochondria
Oxidative phosphorylation
description 24 p.-7 fig.
publishDate 2005
dc.date.none.fl_str_mv 2005
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/377957
url http://hdl.handle.net/10261/377957
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1111/j.1742-4658.2005.04928.x
No
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv John Wiley & Sons
publisher.none.fl_str_mv John Wiley & Sons
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_ 1869422069073051648
score 15.812429

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