Sinigalia, ElisaAlvisi, GualtieroMercorelli, BeatriceCoen, Donald M.Pari, Gregory S.Jans, David A.Ripalti, AlessandroPalù, GiorgioLoregian, Arianna2019-10-052008Sinigalia, 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.01193-08.0022-538X1070-63211098-5514http://nrs.harvard.edu/urn-3:HUL.InstRepos:41482951The 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.en-USJournal Article2019-10-0510.1128/JVI.01193-08