Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120

44 Pags.- 15 Figs.- 2 Tabls. The definitive version is available at: http://www.biochemj.org/

Detalles Bibliográficos
Autores: Sein-Echaluce, Violeta C., Pallarés, María Carmen, Lostao, Anabel, Yruela Guerrero, Inmaculada, Velázquez-Campoy, Adrián, Peleato Sánchez, María Luisa, Fillat, María F.
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2018
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/158968
Acceso en línea:http://hdl.handle.net/10261/158968
Access Level:acceso abierto
Palabra clave:Cyanobacteria
FurB/Zur
Zinc homeostasis
redox sensing
heme binding
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spelling Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120Sein-Echaluce, Violeta C.Pallarés, María CarmenLostao, AnabelYruela Guerrero, InmaculadaVelázquez-Campoy, AdriánPeleato Sánchez, María LuisaFillat, María F.CyanobacteriaFurB/ZurZinc homeostasisredox sensingheme binding44 Pags.- 15 Figs.- 2 Tabls. The definitive version is available at: http://www.biochemj.org/FUR (Ferric uptake regulator) proteins are among the most important families of transcriptional regulators in prokaryotes, often behaving as global regulators. In the cyanobacterium Anabaena PCC 7120, FurB (Zur, Zinc uptake regulator) controls zinc and redox homeostasis through the repression of target genes in a zinc-dependent manner. In vitro, non-specific binding of FurB to DNA elicits protection against oxidative damage and avoids cleavage by deoxyribonuclease I. The present study provides, for the first time, evidence of the influence of redox environment in the interaction of FurB with regulatory zinc and its consequences in FurB–DNA-binding affinity. Calorimetry studies showed that, in addition to one structural Zn(II), FurB is able to bind two additional Zn(II) per monomer and demonstrated the implication of cysteine C93 in regulatory Zn(II) coordination. The interaction of FurB with the second regulatory zinc occurred only under reducing conditions. While non-specific FurB–DNA interaction is Zn(II)-independent, the optimal binding of FurB to target promoters required loading of two regulatory zinc ions. Those results combined with site-directed mutagenesis and gel-shift assays evidenced that the redox state of cysteine C93 conditions the binding of the second regulatory Zn(II) and, in turn, modulates the affinity for a specific DNA target. Furthermore, differential spectroscopy studies showed that cysteine C93 could also be involved in heme coordination by FurB, either as a direct ligand or being located near the binding site. The results indicate that besides controlling zinc homeostasis, FurB could work as a redox-sensing protein probably modifying its zinc and DNA-binding abilities depending upon environmental conditions.This work has been supported by grants B18 from Gobierno de Aragón, BFU2012- 31458/FEDER & BFU2016-77671-P/FEDER from MINECO and UZ2016-BIO-02 from University of Zaragoza. VCS was recipient of a fellowship from Gobierno de Aragón.Peer reviewedPortland PressGobierno de AragónEuropean CommissionMinisterio de Economía y Competitividad (España)Universidad de ZaragozaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201820182018info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/158968reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1042/BCJ20170692Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1589682026-05-22T06:33:51Z
dc.title.none.fl_str_mv Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
title Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
spellingShingle Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
Sein-Echaluce, Violeta C.
Cyanobacteria
FurB/Zur
Zinc homeostasis
redox sensing
heme binding
title_short Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
title_full Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
title_fullStr Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
title_full_unstemmed Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
title_sort Molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120
dc.creator.none.fl_str_mv Sein-Echaluce, Violeta C.
Pallarés, María Carmen
Lostao, Anabel
Yruela Guerrero, Inmaculada
Velázquez-Campoy, Adrián
Peleato Sánchez, María Luisa
Fillat, María F.
author Sein-Echaluce, Violeta C.
author_facet Sein-Echaluce, Violeta C.
Pallarés, María Carmen
Lostao, Anabel
Yruela Guerrero, Inmaculada
Velázquez-Campoy, Adrián
Peleato Sánchez, María Luisa
Fillat, María F.
author_role author
author2 Pallarés, María Carmen
Lostao, Anabel
Yruela Guerrero, Inmaculada
Velázquez-Campoy, Adrián
Peleato Sánchez, María Luisa
Fillat, María F.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Gobierno de Aragón
European Commission
Ministerio de Economía y Competitividad (España)
Universidad de Zaragoza
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Cyanobacteria
FurB/Zur
Zinc homeostasis
redox sensing
heme binding
topic Cyanobacteria
FurB/Zur
Zinc homeostasis
redox sensing
heme binding
description 44 Pags.- 15 Figs.- 2 Tabls. The definitive version is available at: http://www.biochemj.org/
publishDate 2018
dc.date.none.fl_str_mv 2018
2018
2018
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/10261/158968
url http://hdl.handle.net/10261/158968
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1042/BCJ20170692
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Portland Press
publisher.none.fl_str_mv Portland Press
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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