Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases

20 páginas, 6 figuras

Detalles Bibliográficos
Autores: Miguel-Romero, Laura, Mideros-Mora, Cristina, Marina, Alberto, Casino, Patricia
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/209736
Acceso en línea:http://hdl.handle.net/10261/209736
Access Level:acceso abierto
Palabra clave:Cis–trans autophosphorylation
Heterodimer production and purification
Histidine kinases
Signal transduction
Two-component systems
X-ray crystallography
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spelling Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine KinasesMiguel-Romero, LauraMideros-Mora, CristinaMarina, AlbertoCasino, PatriciaCis–trans autophosphorylationHeterodimer production and purificationHistidine kinasesSignal transductionTwo-component systemsX-ray crystallography20 páginas, 6 figurasAutophosphorylation of histidine kinases (HK) is the first step for signal transduction in bacterial two-component signalling systems. As HKs dimerize, the His residue is phosphorylated in cis or trans depending on whether the ATP molecule used in the reaction is bound to the same or the neighboring subunit, respectively. The cis or trans autophosphorylation results from an alternative directionality in the connection between helices α1 and α2 in the HK DHp domain, in such a way that α2 could be oriented almost 90° counterclockwise or clockwise with respect to α1. Sequence and length variability of this connection appears to lie behind the different directionality and is implicated in partner recognition with the response regulator (RR), highlighting its importance in signal transduction. Despite this mechanistic difference, HK autophosphorylation appears to be universal, involving conserved residues neighboring the phosphoacceptor His residue. Herein, we describe a simple protocol to determine both autophosphorylation directionality of HKs and the roles of the catalytic residues in these protein kinases.This work was supported by Spanish Government (Ministry of Economy and Competitiveness) grants BIO2016-78571-P to A.M and BFU2016-78606-P to P.C. is the recipient of a Ramón y Cajal contract, from the Ministry of Economy and Competitiveness. C.M-M is the recipient of a PhD fellowship from the Progama de becas, Secretaría de Educación Superior, Ciencia, Tecnología e Innovación of Ecuador Government (2015-AR2Q9228)Peer reviewedSpringer NatureMinisterio de Economía y Competitividad (España)Secretaría de Educación Superior, Ciencia, Tecnología e Innovación (Ecuador)Marina, Alberto [0000-0002-1334-5273]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202020202020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/209736reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-78571-Pinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2016-78606-Phttp://dx.doi.org/10.1007/978-1-4939-9884-5_9Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2097362026-05-22T06:33:51Z
dc.title.none.fl_str_mv Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
title Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
spellingShingle Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
Miguel-Romero, Laura
Cis–trans autophosphorylation
Heterodimer production and purification
Histidine kinases
Signal transduction
Two-component systems
X-ray crystallography
title_short Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
title_full Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
title_fullStr Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
title_full_unstemmed Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
title_sort Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases
dc.creator.none.fl_str_mv Miguel-Romero, Laura
Mideros-Mora, Cristina
Marina, Alberto
Casino, Patricia
author Miguel-Romero, Laura
author_facet Miguel-Romero, Laura
Mideros-Mora, Cristina
Marina, Alberto
Casino, Patricia
author_role author
author2 Mideros-Mora, Cristina
Marina, Alberto
Casino, Patricia
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Secretaría de Educación Superior, Ciencia, Tecnología e Innovación (Ecuador)
Marina, Alberto [0000-0002-1334-5273]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Cis–trans autophosphorylation
Heterodimer production and purification
Histidine kinases
Signal transduction
Two-component systems
X-ray crystallography
topic Cis–trans autophosphorylation
Heterodimer production and purification
Histidine kinases
Signal transduction
Two-component systems
X-ray crystallography
description 20 páginas, 6 figuras
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
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/10261/209736
url http://hdl.handle.net/10261/209736
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#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2016-78571-P
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2016-78606-P
http://dx.doi.org/10.1007/978-1-4939-9884-5_9
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Springer Nature
publisher.none.fl_str_mv Springer Nature
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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