Role of Homodimerization of Human Cytomegalovirus DNA Polymerase Accessory Protein UL44 in Origin-Dependent DNA Replication in Cells
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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.
2003 ◽
Vol 77
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pp. 8336-8344
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2004 ◽
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pp. 158-167
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1986 ◽
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pp. 2869-2873
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2003 ◽
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pp. 3734-3748
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2016 ◽
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pp. E7818-E7827
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2005 ◽
Vol 79
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pp. 8661-8664
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