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OrpR is a σ54-dependent activator using an iron-sulfur cluster for redox sensing in Desulfovibrio vulgaris Hildenborough

2021-07Artigo científico Acesso aberto
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dc.contributor.authorFiévet, Anouchka
dc.contributor.authorMerrouch, Meriem
dc.contributor.authorBrasseur, Gaël
dc.contributor.authorEve, Danaé
dc.contributor.authorBiondi, Emanuele G.
dc.contributor.authorValette, Odile
dc.contributor.authorPauleta, Sofia R.
dc.contributor.authorDolla, Alain
dc.contributor.authorDermoun, Zorah
dc.contributor.authorBurlat, Bénédicte
dc.contributor.authorAubert, Corinne
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.pblWiley
dc.date.accessioned2021-11-29T23:39:30Z
dc.date.available2021-11-29T23:39:30Z
dc.date.issued2021-07
dc.descriptionSFCT‐ANR/BBB‐MET/0023/2012 IAP7/44, iPROS project) COST Action CA15133
dc.description.abstractEnhancer binding proteins (EBPs) are key players of σ54-regulation that control transcription in response to environmental signals. In the anaerobic microorganism Desulfovibrio vulgaris Hildenborough (DvH), orp operons have been previously shown to be coregulated by σ54-RNA polymerase, the integration host factor IHF and a cognate EBP, OrpR. In this study, ChIP-seq experiments indicated that the OrpR regulon consists of only the two divergent orp operons. In vivo data revealed that (i) OrpR is absolutely required for orp operons transcription, (ii) under anaerobic conditions, OrpR binds on the two dedicated DNA binding sites and leads to high expression levels of the orp operons, (iii) increasing the redox potential of the medium leads to a drastic down-regulation of the orp operons expression. Moreover, combining functional and biophysical studies on the anaerobically purified OrpR leads us to propose that OrpR senses redox potential variations via a redox-sensitive [4Fe–4S]2+ cluster in the sensory PAS domain. Overall, the study herein presents the first characterization of a new Fe–S redox regulator belonging to the σ54-dependent transcriptional regulator family probably advantageously selected by cells adapted to the anaerobic lifestyle to monitor redox stress conditions.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent14
dc.format.extent1218455
dc.identifier.doi10.1111/mmi.14705
dc.identifier.issn0950-382X
dc.identifier.otherPURE: 34405395
dc.identifier.otherPURE UUID: 667b3719-1318-46ff-9c31-e41ba912f598
dc.identifier.otherScopus: 85101553149
dc.identifier.otherPubMed: 33595838
dc.identifier.otherPubMedCentral: PMC8359166
dc.identifier.otherWOS: 000621389200001
dc.identifier.otherORCID: /0000-0002-2149-9416/work/103949214
dc.identifier.urihttp://hdl.handle.net/10362/128455
dc.identifier.urlhttps://www.scopus.com/pages/publications/85101553149
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
dc.relationApplied Molecular Biosciences Unit
dc.relationApplied Molecular Biosciences Unit
dc.subjectanaerobes
dc.subjectDesulfovibrio
dc.subjectenhancer binding protein
dc.subjectiron-sulfur protein
dc.subjectredox sensor
dc.subjecttranscriptional regulator
dc.subjectMicrobiology
dc.subjectMolecular Biology
dc.titleOrpR is a σ54-dependent activator using an iron-sulfur cluster for redox sensing in Desulfovibrio vulgaris Hildenboroughen
dc.typejournal article
degois.publication.firstPage231
degois.publication.issue1
degois.publication.lastPage244
degois.publication.titleMolecular Microbiology
degois.publication.volume116
dspace.entity.typePublication
oaire.awardNumberUIDP/04378/2020
oaire.awardNumberUIDB/04378/2020
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublication38373452-5c9c-4724-8def-f03314ecce0e
relation.isProjectOfPublicatione07cf232-4705-4b5b-b2c4-af8f25311076
relation.isProjectOfPublication.latestForDiscovery38373452-5c9c-4724-8def-f03314ecce0e

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