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Protein-protein interactions leading to recruitment of the host DNA sliding clamp by the hyperthermophilic Sulfolobus islandicus rod- shaped virus 2

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dc.contributor.authorGardner, A.F.
dc.contributor.authorBell, S.D.
dc.contributor.authorWhite, M.F.
dc.contributor.authorPrangishvili, D.
dc.contributor.authorKrupovic, M.
dc.date.accessioned2014-07-17T10:31:01Z
dc.date.available2014-07-17T10:31:01Z
dc.date.issued2014-06-01
dc.identifier132879760
dc.identifiere6c7a02a-8e67-40bb-b1b8-5fd4dcaf54f8
dc.identifier84901290879
dc.identifier000336895600049
dc.identifier.citationGardner , A F , Bell , S D , White , M F , Prangishvili , D & Krupovic , M 2014 , ' Protein-protein interactions leading to recruitment of the host DNA sliding clamp by the hyperthermophilic Sulfolobus islandicus rod- shaped virus 2 ' , Journal of Virology , vol. 88 , no. 12 , pp. 7105-7108 . https://doi.org/10.1128/JVI.00636-14en
dc.identifier.issn0022-538X
dc.identifier.otherORCID: /0000-0003-1543-9342/work/47136122
dc.identifier.urihttps://hdl.handle.net/10023/5037
dc.description.abstractViruses infecting hyperthermophilic archaea typically do not encode DNA polymerases, raising questions regarding their genome replication. Here, using a yeast two-hybrid approach, we have assessed interactions between proteins of Sulfolobus islandicus rod-shaped virus 2 (SIRV2) and the host-encoded proliferating cell nuclear antigen (PCNA), a key DNA replication protein in archaea. Five SIRV2 proteins were found to interact with PCNA, providing insights into the recruitment of host replisome for viral DNA replication.
dc.format.extent4
dc.format.extent780035
dc.language.isoeng
dc.relation.ispartofJournal of Virologyen
dc.subjectQH301 Biologyen
dc.subject.lccQH301en
dc.titleProtein-protein interactions leading to recruitment of the host DNA sliding clamp by the hyperthermophilic Sulfolobus islandicus rod- shaped virus 2en
dc.typeJournal articleen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doi10.1128/JVI.00636-14
dc.description.statusPeer revieweden


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