Open AccessInteraction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha.
Author(s) -
Sam S.-K. Lee,
Qun Dong,
T. S. F. Wang,
I. R. Lehman
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.17.7882
Subject(s) - single stranded binding protein , primase , dna polymerase ii , dna polymerase , dna clamp , replication protein a , biology , microbiology and biotechnology , replication factor c , dna replication , hmg box , dna polymerase i , dna polymerase delta , ddb1 , ter protein , polymerase , eukaryotic dna replication , dna binding protein , dna , biochemistry , gene , reverse transcriptase , rna , transcription factor
The herpes simplex virus 1 (HSV-1) genome encodes seven polypeptides that are required for its replication. These include a heterodimeric DNA polymerase, a single-strand-DNA-binding protein, a heterotrimeric helicase/primase, and a protein (UL9 protein) that binds specifically to an HSV-1 origin of replication (oris). We demonstrate here that UL9 protein interacts specifically with the 180-kDa catalytic subunit of the cellular DNA polymerase alpha-primase. This interaction can be detected by immunoprecipitation with antibodies directed against either of these proteins, by gel mobility shift of an oris-UL9 protein complex, and by stimulation of DNA polymerase activity by the UL9 protein. These findings suggest that enzymes required for cellular DNA replication also participate in HSV-1 DNA replication.