Role of Homodimerization of Human Cytomegalovirus DNA Polymerase Accessory Protein UL44 in Origin-Dependent DNA Replication in Cells

 
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Sinigalia, Elisa
Alvisi, Gualtiero
Mercorelli, Beatrice
Coen, Donald M.
Pari, Gregory S.
Jans, David A.
Ripalti, Alessandro
Palù, Giorgio
Loregian, Arianna
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https://doi.org/10.1128/JVI.01193-08
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Sinigalia, E., G. Alvisi, B. Mercorelli, D. M. Coen, G. S. Pari, D. A. Jans, A. Ripalti, G. Palu, and A. Loregian. 2008. “Role of Homodimerization of Human Cytomegalovirus DNA Polymerase Accessory Protein UL44 in Origin-Dependent DNA Replication in Cells.” Journal of Virology 82 (24): 12574–79. https://doi.org/10.1128/jvi.01193-08.
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.
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