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The Structure of theCyprinid herpesvirus 3ORF112-Zα·Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of Interferon Response

2015-12-25Journal article Open access
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dc.contributor.authorKuś, Krzysztof
dc.contributor.authorRakus, Krzysztof
dc.contributor.authorBoutier, Maxime
dc.contributor.authorTsigkri, Theokliti
dc.contributor.authorGabriel, Luisa
dc.contributor.authorVanderplasschen, Alain
dc.contributor.authorAthanasiadis, Alekos
dc.date.accessioned2016-05-20T12:13:39Z
dc.date.available2016-12-25T01:30:09Z
dc.date.issued2015-12-25
dc.description.abstractIn vertebrate species, the innate immune system down-regulates protein translation in response to viral infection through the action of the double-stranded RNA (dsRNA)-activated protein kinase (PKR). In some teleost species another protein kinase, Z-DNA-dependent protein kinase (PKZ), plays a similar role but instead of dsRNA binding domains, PKZ has Zα domains. These domains recognize the left-handed conformer of dsDNA and dsRNA known as Z-DNA/Z-RNA. Cyprinid herpesvirus 3 infects common and koi carp, which have PKZ, and encodes the ORF112 protein that itself bears a Zα domain, a putative competitive inhibitor of PKZ. Here we present the crystal structure of ORF112-Zα in complex with an 18-bp CpG DNA repeat, at 1.5 Å. We demonstrate that the bound DNA is in the left-handed conformation and identify key interactions for the specificity of ORF112. Localization of ORF112 protein in stress granules induced in Cyprinid herpesvirus 3-infected fish cells suggests a functional behavior similar to that of Zα domains of the interferon-regulated, nucleic acid surveillance proteins ADAR1 and DAI.pt_PT
dc.description.sponsorshipFCT grants: PTDC/BIA-PRO/112962/2009; IF/00641/2013; SFRH/BD/51626/2011.pt_PT
dc.identifier.citationKrzysztof Kuś, Krzysztof Rakus, Maxime Boutier, Theokliti Tsigkri, Luisa Gabriel, Alain Vanderplasschen, and Alekos Athanasiadis The Structure of the Cyprinid herpesvirus 3 ORF112-Zα·Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of Interferon Response J. Biol. Chem. 2015 290: 30713-. doi:10.1074/jbc.M115.679407pt_PT
dc.identifier.doi10.1074/jbc.M115.679407pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/611
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherhttp://www.jbc.org/content/290/52/30713pt_PT
dc.relationTransnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities
dc.relation.publisherversionhttp://www.jbc.org/content/290/52/30713pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAmino Acid Sequencept_PT
dc.subjectAnimalspt_PT
dc.subjectBinding Sitespt_PT
dc.subjectCarpspt_PT
dc.subjectConserved Sequencept_PT
dc.subjectDNA, Z-Formpt_PT
dc.subjectDNA-Activated Protein Kinasept_PT
dc.subjectFish Diseasespt_PT
dc.subjectInterferonspt_PT
dc.subjectModels, Molecularpt_PT
dc.subjectNucleic Acid Conformationpt_PT
dc.subjectPoxviridaept_PT
dc.subjectProtein Bindingpt_PT
dc.subjectProtein Structure, Tertiarypt_PT
dc.subjectRNA Virusespt_PT
dc.subjectRNA, Double-Strandedpt_PT
dc.subjectViral Proteinspt_PT
dc.titleThe Structure of theCyprinid herpesvirus 3ORF112-Zα·Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of Interferon Responsept_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleTransnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/283570/EU
oaire.citation.endPage30725pt_PT
oaire.citation.issue52pt_PT
oaire.citation.startPage30713pt_PT
oaire.citation.titleJournal of Biological Chemistrypt_PT
oaire.citation.volume290pt_PT
oaire.fundingStreamFP7
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublication378ed56f-61ec-4eea-8f16-9dbec5ca3bed
relation.isProjectOfPublication.latestForDiscovery378ed56f-61ec-4eea-8f16-9dbec5ca3bed

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