Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase

9 pags., 8 figs.

Detalles Bibliográficos
Autores: Ziebarth, Tawn D., González-Soltero, Rocio, Makowska-Grzyska, Magdalena M., Núñez-Ramírez, Rafael, Carazo, José M., Kaguni, Laurie S.
Tipo de recurso: artículo
Fecha de publicación:2010
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/246480
Acceso en línea:http://hdl.handle.net/10261/246480
Access Level:acceso abierto
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spelling Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicaseZiebarth, Tawn D.González-Soltero, RocioMakowska-Grzyska, Magdalena M.Núñez-Ramírez, RafaelCarazo, José M.Kaguni, Laurie S.9 pags., 8 figs.We examined the effects of cofactors and DNA on the stability, oligomeric state and conformation of the human mitochondrial DNA helicase. We demonstrate that low salt conditions result in protein aggregation that may cause dissociation of oligomeric structure. The low salt sensitivity of the mitochondrial DNA helicase is mitigated by the presence of magnesium, nucleotide, and increased temperature. Electron microscopic and glutaraldehyde cross-linking analyses provide the first evidence of a heptameric oligomer and its interconversion from a hexameric form. Limited proteolysis by trypsin shows that binding of nucleoside triphosphate produces a conformational change that is distinct from the conformation observed in the presence of nucleoside diphosphate. We find that single-stranded DNA binding occurs in the absence of cofactors and renders the mitochondrial DNA helicase more susceptible to proteolytic digestion. Our studies indicate that the human mitochondrial DNA helicase shares basic properties with the SF4 replicative helicases, but also identify common features with helicases outside the superfamily, including dynamic conformations similar to other AAA+ ATPases. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.This work was supported, in whole or in part, by Grant GM45295 from the National Institutes of Health (to L. S. K.). This work was also supported by Grants CSD2006-00023 and BIO2007-67150-C03-1 from MEC and S-GEN0166-2006 from CAM (to J.-M. C.).American Society for Biochemistry and Molecular BiologyNational Institutes of Health (US)Ministerio de Educación y Ciencia (España)Comunidad de MadridConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2021202120102021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/246480reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#S-GEN0166-2006/CMMEC/BIO2007-67150-C03-1http://dx.doi.org/10.1074/jbc.M109.099663Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2464802026-05-22T06:33:51Z
dc.title.none.fl_str_mv Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
title Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
spellingShingle Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
Ziebarth, Tawn D.
title_short Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
title_full Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
title_fullStr Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
title_full_unstemmed Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
title_sort Dynamic effects of cofactors and DNA on the oligomeric state of human mitochondrial DNA helicase
dc.creator.none.fl_str_mv Ziebarth, Tawn D.
González-Soltero, Rocio
Makowska-Grzyska, Magdalena M.
Núñez-Ramírez, Rafael
Carazo, José M.
Kaguni, Laurie S.
author Ziebarth, Tawn D.
author_facet Ziebarth, Tawn D.
González-Soltero, Rocio
Makowska-Grzyska, Magdalena M.
Núñez-Ramírez, Rafael
Carazo, José M.
Kaguni, Laurie S.
author_role author
author2 González-Soltero, Rocio
Makowska-Grzyska, Magdalena M.
Núñez-Ramírez, Rafael
Carazo, José M.
Kaguni, Laurie S.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv National Institutes of Health (US)
Ministerio de Educación y Ciencia (España)
Comunidad de Madrid
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description 9 pags., 8 figs.
publishDate 2010
dc.date.none.fl_str_mv 2010
2021
2021
2021
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/10261/246480
url http://hdl.handle.net/10261/246480
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#
S-GEN0166-2006/CM
MEC/BIO2007-67150-C03-1
http://dx.doi.org/10.1074/jbc.M109.099663
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
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score 15,811543

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