Open AccessThe Carboxy-Terminal Segment of the Human Cytomegalovirus DNA Polymerase Accessory Subunit UL44 Is Crucial for Viral Replication
Author(s) -
Laurie A. Silva,
Arianna Loregian,
Gregory S. Pari,
Blair L. Strang,
Donald M. Coen
Publication year - 2010
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01033-10
Subject(s) - biology , polymerase , viral replication , dna replication , dna polymerase , virology , terminal (telecommunication) , protein subunit , replication (statistics) , dna clamp , microbiology and biotechnology , dna polymerase ii , replication factor c , genetics , eukaryotic dna replication , dna , polymerase chain reaction , virus , reverse transcriptase , gene , telecommunications , computer science
The amino-terminal 290 residues of UL44, the presumed processivity factor of human cytomegalovirus DNA polymerase, possess all of the established biochemical activities of the full-length protein, while the carboxy-terminal 143 residues contain a nuclear localization signal (NLS). We found that although the amino-terminal domain was sufficient for origin-dependent synthesis in a transient-transfection assay, the carboxy-terminal segment was crucial for virus replication and for the formation of DNA replication compartments in infected cells, even when this segment was replaced with a simian virus 40 NLS that ensured nuclear localization. Our results suggest a role for this segment in viral DNA synthesis.