Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein

DNA replication is essential to all living organisms as it ensures the fidelity of genetic material for the next generation of dividing cells. One of the simplest replication initiation mechanisms is the rolling circle replication. In the streptococcal plasmid pMV158, which confers antibiotic resist...

Descripción completa

Detalles Bibliográficos
Autores: Machón Sobrado, Cristina, Ruiz Masó, José Angel, Amodio, Juliana, Boer. D. Roeland, Bordanaba Ruiseco, Lorena, Bury, Katarzyna, Konieczny, Igor, Solar, Gloria del, Coll Capella, Miquel, 1955-
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/200288
Acceso en línea:https://hdl.handle.net/2445/200288
Access Level:acceso abierto
Palabra clave:Duplicació de l'ADN
Plasmidis
DNA replication
Plasmids
id ES_6b19bd383aa5ec69f3342a68a28bbce2
oai_identifier_str oai:recercat.cat:2445/200288
network_acronym_str ES
network_name_str España
repository_id_str
spelling Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function proteinMachón Sobrado, CristinaRuiz Masó, José AngelAmodio, JulianaBoer. D. RoelandBordanaba Ruiseco, LorenaBury, KatarzynaKonieczny, IgorSolar, Gloria delColl Capella, Miquel, 1955-Duplicació de l'ADNPlasmidisDNA replicationPlasmidsDNA replication is essential to all living organisms as it ensures the fidelity of genetic material for the next generation of dividing cells. One of the simplest replication initiation mechanisms is the rolling circle replication. In the streptococcal plasmid pMV158, which confers antibiotic resistance to tetracycline, replication initiation is catalysed by RepB protein. The RepB N-terminal domain or origin binding domain binds to the recognition sequence (bind locus) of the double-strand origin of replication and cleaves one DNA strand at a specific site within the nic locus. Using biochemical and crystallographic analyses, here we show how the origin binding domain recognises and binds to the bind locus using structural elements removed from the active site, namely the recognition α helix, and a β-strand that organises upon binding. A new hexameric structure of full-length RepB that highlights the great flexibility of this protein is presented, which could account for its ability to perform different tasks, namely bind to two distinct loci and cleave one strand of DNA at the plasmid origin.© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.Oxford University Press2023202320232023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion15 p.application/pdfhttps://hdl.handle.net/2445/200288Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona))reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.1093/nar/gkac1271Nucleic Acids Research, 2023, vol. 51, num. 3, p. 1458-1472https://doi.org/10.1093/nar/gkac1271cc by (c) Machón Sobrado, Cristina et al., 2023http://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/2002882026-05-29T05:05:01Z
dc.title.none.fl_str_mv Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
title Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
spellingShingle Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
Machón Sobrado, Cristina
Duplicació de l'ADN
Plasmidis
DNA replication
Plasmids
title_short Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
title_full Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
title_fullStr Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
title_full_unstemmed Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
title_sort Structures of pMV158 replication initiator RepB with and without DNA reveal a flexible dual-function protein
dc.creator.none.fl_str_mv Machón Sobrado, Cristina
Ruiz Masó, José Angel
Amodio, Juliana
Boer. D. Roeland
Bordanaba Ruiseco, Lorena
Bury, Katarzyna
Konieczny, Igor
Solar, Gloria del
Coll Capella, Miquel, 1955-
author Machón Sobrado, Cristina
author_facet Machón Sobrado, Cristina
Ruiz Masó, José Angel
Amodio, Juliana
Boer. D. Roeland
Bordanaba Ruiseco, Lorena
Bury, Katarzyna
Konieczny, Igor
Solar, Gloria del
Coll Capella, Miquel, 1955-
author_role author
author2 Ruiz Masó, José Angel
Amodio, Juliana
Boer. D. Roeland
Bordanaba Ruiseco, Lorena
Bury, Katarzyna
Konieczny, Igor
Solar, Gloria del
Coll Capella, Miquel, 1955-
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Duplicació de l'ADN
Plasmidis
DNA replication
Plasmids
topic Duplicació de l'ADN
Plasmidis
DNA replication
Plasmids
description DNA replication is essential to all living organisms as it ensures the fidelity of genetic material for the next generation of dividing cells. One of the simplest replication initiation mechanisms is the rolling circle replication. In the streptococcal plasmid pMV158, which confers antibiotic resistance to tetracycline, replication initiation is catalysed by RepB protein. The RepB N-terminal domain or origin binding domain binds to the recognition sequence (bind locus) of the double-strand origin of replication and cleaves one DNA strand at a specific site within the nic locus. Using biochemical and crystallographic analyses, here we show how the origin binding domain recognises and binds to the bind locus using structural elements removed from the active site, namely the recognition α helix, and a β-strand that organises upon binding. A new hexameric structure of full-length RepB that highlights the great flexibility of this protein is presented, which could account for its ability to perform different tasks, namely bind to two distinct loci and cleave one strand of DNA at the plasmid origin.© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/200288
url https://hdl.handle.net/2445/200288
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1093/nar/gkac1271
Nucleic Acids Research, 2023, vol. 51, num. 3, p. 1458-1472
https://doi.org/10.1093/nar/gkac1271
dc.rights.none.fl_str_mv cc by (c) Machón Sobrado, Cristina et al., 2023
http://creativecommons.org/licenses/by/3.0/es/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc by (c) Machón Sobrado, Cristina et al., 2023
http://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 15 p.
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 Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona))
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869410159930900480
score 15,81155

Similares en LA Referencia