Journal
JOURNAL OF VIROLOGY
Volume 82, Issue 24, Pages 12574-12579Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01193-08
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Funding
- PRIN 2005 [2005060941]
- MURST EX60%
- University of Bologna
- Italian Ministry of Education
- Italian Ministry of Public Health
- NHMRC (Australia) SPRF fellowship [384109]
- NIH [AI19838]
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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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