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dc.contributor.authorPeeters, Eveline
dc.contributor.authorBoon, Maarten
dc.contributor.authorRollie, Clare Jane Catherine
dc.contributor.authorWillaert, Ronnie G.
dc.contributor.authorVoet, Marleen
dc.contributor.authorWhite, Malcolm Frederick
dc.contributor.authorPrangishvili, David
dc.contributor.authorLavigne, Rob
dc.contributor.authorQuax, Tessa E. F.
dc.date.accessioned2017-07-18T15:30:10Z
dc.date.available2017-07-18T15:30:10Z
dc.date.issued2017-07
dc.identifier.citationPeeters , E , Boon , M , Rollie , C J C , Willaert , R G , Voet , M , White , M F , Prangishvili , D , Lavigne , R & Quax , T E F 2017 , ' DNA‐Interacting characteristics of the archaeal Rudiviral protein SIRV2_Gp1 ' , Viruses , vol. 9 , no. 7 , 190 . https://doi.org/10.3390/v9070190en
dc.identifier.issn1999-4915
dc.identifier.otherPURE: 250537150
dc.identifier.otherPURE UUID: 9570f000-93ef-4f03-86f7-a408774a9063
dc.identifier.otherScopus: 85025625256
dc.identifier.otherORCID: /0000-0003-1543-9342/work/47136109
dc.identifier.otherWOS: 000406684400032
dc.identifier.urihttp://hdl.handle.net/10023/11250
dc.description.abstractWhereas the infection cycles of many bacterial and eukaryotic viruses have been characterized in detail, those of archaeal viruses remain largely unexplored. Recently, studies on a few model archaeal viruses such as SIRV2 (Sulfolobus islandicus rod‐shaped virus) have revealed an unusual lysis mechanism that involves the formation of pyramidal egress structures on the host cell surface. To expand understanding of the infection cycle of SIRV2, we aimed to functionally characterize gp1, which is a SIRV2 gene with unknown function. The SIRV2_Gp1 protein is highly expressed during early stages of infection and it is the only protein that is encoded twice on the viral genome. It harbours a helix‐turn‐helix motif and was therefore hypothesized to bind DNA. The DNA‐binding behavior of SIRV2_Gp1 was characterized with electrophoretic mobility shift assays and atomic force microscopy. We provide evidence that the protein interacts with DNA and that it forms large aggregates, thereby causing extreme condensation of the DNA. Furthermore, the N‐terminal domain of the protein mediates toxicity to the viral host Sulfolobus. Our findings may lead to biotechnological applications, such as the development of a toxic peptide for the containment of pathogenic bacteria, and add to our understanding of the Rudiviral infection cycle.
dc.format.extent13
dc.language.isoeng
dc.relation.ispartofVirusesen
dc.rights© 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).en
dc.subjectArchaeaen
dc.subjectArchaeal virusen
dc.subjectRudiviridaeen
dc.subjectSIRV2en
dc.subjectSolfolobusen
dc.subjectDNA bindingen
dc.subjectHelix-turn-helix domanen
dc.subjectQH301 Biologyen
dc.subjectQR355 Virologyen
dc.subjectNDASen
dc.subject.lccQH301en
dc.subject.lccQR355en
dc.titleDNA‐Interacting characteristics of the archaeal Rudiviral protein SIRV2_Gp1en
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.3390/v9070190
dc.description.statusPeer revieweden


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