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dc.contributor.authorQuyen, Dong Van
dc.contributor.authorHa, Sung Chul
dc.contributor.authorKim, Kyeong Kyu
dc.contributor.authorKim, Yang-Gyun
dc.contributor.authorLowenhaupt, Ky
dc.contributor.authorRich, Alexander
dc.date.accessioned2012-06-01T19:57:28Z
dc.date.available2012-06-01T19:57:28Z
dc.date.issued2007-11
dc.date.submitted2007-09
dc.identifier.issn0305-1048
dc.identifier.issn1362-4962
dc.identifier.urihttp://hdl.handle.net/1721.1/70997
dc.description.abstractThe E3L gene is essential for pathogenesis in vaccinia virus. The E3L gene product consists of an N-terminal Zα domain and a C-terminal double-stranded RNA (dsRNA) binding domain; the left-handed Z-DNA-binding activity of the Zα domain of E3L is required for viral pathogenicity in mice. E3L is highly conserved among poxviruses, including the smallpox virus, and it is likely that the orthologous Zα domains play similar roles. To better understand the biological function of E3L proteins, we have investigated the Z-DNA-binding behavior of five representative Zα domains from poxviruses. Using surface plasmon resonance (SPR), we have demonstrated that these viral Zα domains bind Z-DNA tightly. Ability of Zα[subscript E3L] converting B-DNA to Z-DNA was measured by circular dichroism (CD). The extents to which these Zαs can stabilize Z-DNA vary considerably. Mutational studies demonstrate that residues in the loop of the β-wing play an important role in this stabilization. Notably the Zα domain of vaccinia E3L acquires ability to convert B-DNA to Z-DNA by mutating amino acid residues in this region. Differences in the host cells of the various poxviruses may require different abilities to stabilize Z-DNA; this may be reflected in the observed differences in behavior in these Zα proteins.en_US
dc.description.sponsorshipKorean Science and Engineering Foundation (National Research Laboratory Program (NRL-2006-02287))en_US
dc.description.sponsorshipKorean Science and Engineering Foundation (Ubiquitome Research Program (M10533010002-06N3301-00210))en_US
dc.description.sponsorshipKorean Science and Engineering Foundation (21C Frontier Functional Proteomics Program (FPR06B2-120))en_US
dc.description.sponsorshipNational Institutes of Health (U.S.)en_US
dc.description.sponsorshipEllison Medical Foundationen_US
dc.description.sponsorshipKorea (South). Ministry of Science and Technology (National Laboratory program (NRL-2006-02287))en_US
dc.language.isoen_US
dc.publisherOxford University Press (OUP)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1093/nar/gkm748en_US
dc.rightsCreative Commons Attribution Non-Commercialen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc/2.5en_US
dc.sourceOxforden_US
dc.titleCharacterization of DNA-binding activity of Zα domains from poxviruses and the importance of the β-wing regions in converting B-DNA to Z-DNAen_US
dc.typeArticleen_US
dc.identifier.citationVan Quyen, D. et al. “Characterization of DNA-binding Activity of Z  Domains from Poxviruses and the Importance of the -wing Regions in Converting B-DNA to Z-DNA.” Nucleic Acids Research 35.22 (2007): 7714–7720. Web. 1 June 2012.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.approverRich, Alexander
dc.contributor.mitauthorLowenhaupt, Ky
dc.contributor.mitauthorRich, Alexander
dc.relation.journalNucleic Acids Researchen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsVan Quyen, D.; Ha, S. C.; Lowenhaupt, K.; Rich, A.; Kim, K. K.; Kim, Y.-G.en
dc.identifier.orcidhttps://orcid.org/0000-0002-8187-6498
mit.licensePUBLISHER_CCen_US
mit.metadata.statusComplete


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