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dc.contributor.authorSilva, Laurie
dc.contributor.authorLoregian, Arianna
dc.contributor.authorPari, Gregory
dc.contributor.authorStrang, Blair
dc.contributor.authorCoen, Donald
dc.date.accessioned2019-10-05T03:27:38Z
dc.date.issued2010
dc.identifier.citationSilva, L. A., A. Loregian, G. S. Pari, B. L. Strang, and D. M. Coen. 2010. “The Carboxy-Terminal Segment of the Human Cytomegalovirus DNA Polymerase Accessory Subunit UL44 Is Crucial for Viral Replication.” Journal of Virology 84 (21): 11563–68. https://doi.org/10.1128/jvi.01033-10.
dc.identifier.issn0022-538X
dc.identifier.issn1070-6321
dc.identifier.issn1098-5514
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41482950*
dc.description.abstractThe amino-terminal 290 residues of UL44, the presumed processivity factor of human cytomegalovirus DNA polymerase, possess all of the established biochemical activities of the full-length protein, while the carboxyterminal 143 residues contain a nuclear localization signal (NLS). We found that although the amino-terminal domain was sufficient for origin-dependent synthesis in a transient-transfection assay, the carboxy-terminal segment was crucial for virus replication and for the formation of DNA replication compartments in infected cells, even when this segment was replaced with a simian virus 40 NLS that ensured nuclear localization. Our results suggest a role for this segment in viral DNA synthesis.
dc.language.isoen_US
dc.publisherAmerican Society for Microbiology
dash.licenseLAA
dc.titleThe Carboxy-Terminal Segment of the Human Cytomegalovirus DNA Polymerase Accessory Subunit UL44 Is Crucial for Viral Replication
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalJournal of Virology
dash.depositing.authorCoen, Donald Mark::f1d1eb8434c5ee0d3e2fa13c1a313e4d::600
dc.date.available2019-10-05T03:27:38Z
dash.workflow.comments1Science Serial ID 63127
dc.identifier.doi10.1128/JVI.01033-10
dash.source.volume84;21
dash.source.page11563


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