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The human parvovirus B19 non-structural protein 1 N-terminal domain specifically binds to the origin of replication in the viral DNA

dc.contributor.authorTewary, Sunil Kumar
dc.contributor.authorZhao, Haiyan
dc.contributor.authorDeng, Xuefeng
dc.contributor.authorQiu, Jianming
dc.contributor.authorTang, Liang
dc.date.accessioned2017-04-10T20:34:44Z
dc.date.available2017-04-10T20:34:44Z
dc.date.issued2013-12-20
dc.identifier.citationTewary, Sunil Kumar et al. “The Human Parvovirus B19 Non-Structural Protein 1 N-Terminal Domain Specifically Binds to the Origin of Replication in the Viral DNA.” Virology 449 (2014): 297–303.en_US
dc.identifier.urihttp://hdl.handle.net/1808/23620
dc.description.abstractThe non-structural protein 1 (NS1) of human parvovirus B19 plays a critical role in viral DNA replication. Previous studies identified the origin of replication in the viral DNA, which contains four DNA elements, namely NSBE1 to NSBE4, that are required for optimal viral replication (Guan et al, 2009, J. Virology, 83, 9541-9553). Here we have demonstrated in vitro that the NS1 N-terminal domain (NS1N) binds to the origin of replication in a sequence-specific, length-dependent manner that requires NSBE1 and NSBE2, while NSBE3 and NSBE4 are dispensable. Mutagenesis analysis has identified nucleotides in NSBE1 and NSBE2 that are critical for NS1N binding. These results suggest that NS1 binds to the NSBE1-NSBE2 region in the origin of replication, while NSBE3 and NSBE4 may provide binding sites for potential cellular factors. Such a specialized nucleoprotein complex may enable NS1 to nick the terminal resolution site and separate DNA strands during replication.en_US
dc.publisherElsevieren_US
dc.rightsThis is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 3.0 (CC BY-NC-ND 3.0 US), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/
dc.subjectParvovirusen_US
dc.subjectB19en_US
dc.subjectNon-structural protein 1en_US
dc.subjectOrigin of replicationen_US
dc.subjectProtein DNA interactionen_US
dc.titleThe human parvovirus B19 non-structural protein 1 N-terminal domain specifically binds to the origin of replication in the viral DNAen_US
dc.typeArticleen_US
kusw.kuauthorTang, Liang
kusw.kudepartmentMolecular Biosciencesen_US
kusw.oanotesPer SHERPA/RoMEO 4/10/2017: Author's Pre-print: green tick author can archive pre-print (ie pre-refereeing) Author's Post-print: green tick author can archive post-print (ie final draft post-refereeing) Publisher's Version/PDF: cross author cannot archive publisher's version/PDF General Conditions: Authors pre-print on any website, including arXiv and RePEC Author's post-print on author's personal website immediately Author's post-print on open access repository after an embargo period of between 12 months and 48 months Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months Author's post-print may be used to update arXiv and RepEC Publisher's version/PDF cannot be used Must link to publisher version with DOI Author's post-print must be released with a Creative Commons Attribution Non-Commercial No Derivatives Licenseen_US
dc.identifier.doi10.1016/j.virol.2013.11.031en_US
dc.identifier.orcidhttps://orcid.org/0000-0001-5812-1866
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 3.0 (CC BY-NC-ND 3.0 US), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
Except where otherwise noted, this item's license is described as: This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 3.0 (CC BY-NC-ND 3.0 US), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.