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J Virol. 2008 Dec;82(24):12574-9. doi: 10.1128/JVI.01193-08. Epub 2008 Oct 8.

Role of homodimerization of human cytomegalovirus DNA polymerase accessory protein UL44 in origin-dependent DNA replication in cells.

Author information

1
Department of Histology, Microbiology and Medical Biotechnologies, University of Padua, via Gabelli 63, 35121 Padua, Italy.

Abstract

The presumed processivity subunit of human cytomegalovirus (HCMV) DNA polymerase, UL44, forms homodimers. The dimerization of UL44 is important for binding to DNA in vitro; however, whether it is also important for DNA replication in a cellular context is unknown. Here we show that UL44 point mutants that are impaired for dimerization, but not for nuclear localization or interaction with the C terminus of the polymerase catalytic subunit, are not capable of supporting HCMV oriLyt-dependent DNA replication in cells. These data suggest that the disruption of UL44 homodimers could represent a novel anti-HCMV strategy.

PMID:
18842734
PMCID:
PMC2593364
DOI:
10.1128/JVI.01193-08
[Indexed for MEDLINE]
Free PMC Article

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