Physical basis for the loading of a bacterial replicative helicase onto DNA

81 p.- 7 fig.-1 tab.-7 fig. supl.-6 vid.

Detalles Bibliográficos
Autores: Arias-Palomo, Ernesto, Puri, Neha, O'Shea Murray, Valerie L., Yan, Qianyun, Berger, James M.
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/179930
Acceso en línea:http://hdl.handle.net/10261/179930
Access Level:acceso abierto
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spelling Physical basis for the loading of a bacterial replicative helicase onto DNAArias-Palomo, ErnestoPuri, NehaO'Shea Murray, Valerie L.Yan, QianyunBerger, James M.81 p.- 7 fig.-1 tab.-7 fig. supl.-6 vid.In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases onto DNA to initiate chromosomal replication. To better understand the mechanisms by which helicase loading can occur, we used cryo-EM to determine sub-4-Å-resolution structures of the E. coli DnaB⋅DnaC helicase⋅loader complex with nucleotide in pre- and post-DNA engagement states. In the absence of DNA, six DnaC protomers latch onto and crack open a DnaB hexamer using an extended N-terminal domain, stabilizing this conformation through nucleotide-dependent ATPase interactions. Upon binding DNA, DnaC hydrolyzes ATP, allowing DnaB to isomerize into a topologically closed, pre-translocation state competent to bind primase. Our data show how DnaC opens the DnaB ring and represses the helicase prior to DNA binding and how DnaC ATPase activity is reciprocally regulated by DnaB and DNA. Comparative analyses reveal how the helicase loading mechanism of DnaC parallels and diverges from homologous AAA+ systems involved in DNA replication and transposition.This work was supported by the NIGMS (to J.M.B., R37-071747), and by the Spanish MINECO/AEI, the ERDF ESF, (to E.A.-P., BFU2017-89143-P and RYC-2015-19059).Access to eBIC was supported by iNEXT, grant number 653706, funded by the Horizon 2020 program of the European Commission.Peer reviewedElsevierMinisterio de Ciencia, Innovación y Universidades (España)Ministerio de Economía y Competitividad (España)European CommissionArias-Palomo, Ernesto [0000-0002-2706-7411]Puri, Neha [0000-0002-7386-5027]Berger, James M. [0000-0003-0666-1240]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201920192019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/179930reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#MICIU/ICTI2017-2020/BFU2017-89143-Pinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/RYC-2015-19059info:eu-repo/grantAgreement/EC/H2020/653706https://doi.org/10.1016/j.molcel.2019.01.023Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1799302026-05-22T06:33:51Z
dc.title.none.fl_str_mv Physical basis for the loading of a bacterial replicative helicase onto DNA
title Physical basis for the loading of a bacterial replicative helicase onto DNA
spellingShingle Physical basis for the loading of a bacterial replicative helicase onto DNA
Arias-Palomo, Ernesto
title_short Physical basis for the loading of a bacterial replicative helicase onto DNA
title_full Physical basis for the loading of a bacterial replicative helicase onto DNA
title_fullStr Physical basis for the loading of a bacterial replicative helicase onto DNA
title_full_unstemmed Physical basis for the loading of a bacterial replicative helicase onto DNA
title_sort Physical basis for the loading of a bacterial replicative helicase onto DNA
dc.creator.none.fl_str_mv Arias-Palomo, Ernesto
Puri, Neha
O'Shea Murray, Valerie L.
Yan, Qianyun
Berger, James M.
author Arias-Palomo, Ernesto
author_facet Arias-Palomo, Ernesto
Puri, Neha
O'Shea Murray, Valerie L.
Yan, Qianyun
Berger, James M.
author_role author
author2 Puri, Neha
O'Shea Murray, Valerie L.
Yan, Qianyun
Berger, James M.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Ministerio de Economía y Competitividad (España)
European Commission
Arias-Palomo, Ernesto [0000-0002-2706-7411]
Puri, Neha [0000-0002-7386-5027]
Berger, James M. [0000-0003-0666-1240]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description 81 p.- 7 fig.-1 tab.-7 fig. supl.-6 vid.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019
2019
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/10261/179930
url http://hdl.handle.net/10261/179930
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#
#PLACEHOLDER_PARENT_METADATA_VALUE#
MICIU/ICTI2017-2020/BFU2017-89143-P
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/RYC-2015-19059
info:eu-repo/grantAgreement/EC/H2020/653706
https://doi.org/10.1016/j.molcel.2019.01.023
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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