NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex

15 p.-6 fig.-2 tab.

Detalles Bibliográficos
Autores: Machado, Luciana E. S. F., Castellen, Patricia, Blasios, Valdir, Ribeiro-Filho, Helder V., Bisson-Filho, Alexandre W., Benites Pariente, Jhonatan S., Nogueira, Maria L. C., Sforça, Maurizio, Honorato, Rodrigo V., Lopes-de-Oliveira, Paulo S., Salinas, Roberto K., Andreu, José Manuel, Zeri, Ana C., Gueiros-Filho, Frederico J.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/390044
Acceso en línea:http://hdl.handle.net/10261/390044
Access Level:acceso abierto
Palabra clave:Bacterial cell division
FtsZ
MinC
NMR
Protein complex prediction
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spelling NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complexMachado, Luciana E. S. F.Castellen, PatriciaBlasios, ValdirRibeiro-Filho, Helder V.Bisson-Filho, Alexandre W.Benites Pariente, Jhonatan S.Nogueira, Maria L. C.Sforça, MaurizioHonorato, Rodrigo V.Lopes-de-Oliveira, Paulo S.Salinas, Roberto K.Andreu, José ManuelZeri, Ana C.Gueiros-Filho, Frederico J.Bacterial cell divisionFtsZMinCNMRProtein complex prediction15 p.-6 fig.-2 tab.The Min system is a key spatial regulator of cell division in rod-shaped bacteria and the first FtsZ-negative modulator to be recognized. Nevertheless, despite extensive genetic and in vitro studies, the molecular mechanism used by MinC to inhibit Z-ring formation remains incompletely understood. The crystallization of FtsZ in complex with other negative regulators such as SulA and MciZ has provided important structural information to corroborate in vitro experiments and establish the mechanism of Z-ring antagonism by these modulators. However, MinC and FtsZ have so far eluded co-crystallization, probably because their complex is too unstable to be crystallized. To gain structural insight into the mechanism of action of MinC, we determined the solution structure of the N-terminal domain of Bacillus subtilis MinC, and through NMR titration experiments and mutagenesis identified the binding interfaces involved in the MinCN-FtsZ interaction. By using our experimental results as restraints in docking, we also constructed a molecular model for the FtsZ:MinCN complex and validated it by molecular dynamics. The model shows that MinCN binding overlaps with the FtsZ polymerization interface on the C-terminal globular subdomain of FtsZ and, thus, provides a structural basis for MinCN inhibition of FtsZ filament formation. Given that the C-terminal polymerization interface of FtsZ corresponds to the plus end of FtsZ filaments, we propose that capping is the main mechanism employed by MinC to antagonize FtsZ polymerization.This work was supported by FAPESP grants 10/51866-0, 16/05203-5, 20/02061-0 (to F.J.G.F) and fellowships 17/17692-3 (to L.E.S.F.M.) and 10/51870-7 (to P.C.), and by the Spanish Ministry of Science (MCIN) grant BFU2014-51823-R (to J.M.A).Peer reviewedElsevierFundação de Amparo à Pesquisa do Estado de São PauloMinisterio de Ciencia e Innovación (España)Castellen, Patricia [0000-0003-4718-740X]Ribeiro-Filho, Helder V. [0000-0001-8471-207X]Bisson-Filho, Alexandre W. [0000-0002-5940-7230]Benites Pariente, Jhonatan S. [0000-0001-6595-0478]Salinas, Roberto K. [0000-0003-1032-7683]Andreu, José Manuel [0000-0001-8064-6933]Gueiros-Filho, Frederico J. [0000-0001-5425-2439]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/390044reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO//BFU2014-51823-Rhttps://doi.org/10.1016/j.jbc.2025.108169Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3900442026-05-22T06:33:51Z
dc.title.none.fl_str_mv NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
title NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
spellingShingle NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
Machado, Luciana E. S. F.
Bacterial cell division
FtsZ
MinC
NMR
Protein complex prediction
title_short NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
title_full NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
title_fullStr NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
title_full_unstemmed NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
title_sort NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex
dc.creator.none.fl_str_mv Machado, Luciana E. S. F.
Castellen, Patricia
Blasios, Valdir
Ribeiro-Filho, Helder V.
Bisson-Filho, Alexandre W.
Benites Pariente, Jhonatan S.
Nogueira, Maria L. C.
Sforça, Maurizio
Honorato, Rodrigo V.
Lopes-de-Oliveira, Paulo S.
Salinas, Roberto K.
Andreu, José Manuel
Zeri, Ana C.
Gueiros-Filho, Frederico J.
author Machado, Luciana E. S. F.
author_facet Machado, Luciana E. S. F.
Castellen, Patricia
Blasios, Valdir
Ribeiro-Filho, Helder V.
Bisson-Filho, Alexandre W.
Benites Pariente, Jhonatan S.
Nogueira, Maria L. C.
Sforça, Maurizio
Honorato, Rodrigo V.
Lopes-de-Oliveira, Paulo S.
Salinas, Roberto K.
Andreu, José Manuel
Zeri, Ana C.
Gueiros-Filho, Frederico J.
author_role author
author2 Castellen, Patricia
Blasios, Valdir
Ribeiro-Filho, Helder V.
Bisson-Filho, Alexandre W.
Benites Pariente, Jhonatan S.
Nogueira, Maria L. C.
Sforça, Maurizio
Honorato, Rodrigo V.
Lopes-de-Oliveira, Paulo S.
Salinas, Roberto K.
Andreu, José Manuel
Zeri, Ana C.
Gueiros-Filho, Frederico J.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Fundação de Amparo à Pesquisa do Estado de São Paulo
Ministerio de Ciencia e Innovación (España)
Castellen, Patricia [0000-0003-4718-740X]
Ribeiro-Filho, Helder V. [0000-0001-8471-207X]
Bisson-Filho, Alexandre W. [0000-0002-5940-7230]
Benites Pariente, Jhonatan S. [0000-0001-6595-0478]
Salinas, Roberto K. [0000-0003-1032-7683]
Andreu, José Manuel [0000-0001-8064-6933]
Gueiros-Filho, Frederico J. [0000-0001-5425-2439]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Bacterial cell division
FtsZ
MinC
NMR
Protein complex prediction
topic Bacterial cell division
FtsZ
MinC
NMR
Protein complex prediction
description 15 p.-6 fig.-2 tab.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/390044
url http://hdl.handle.net/10261/390044
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO//BFU2014-51823-R
https://doi.org/10.1016/j.jbc.2025.108169

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
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