Characterization of Herpes Simplex Virus-induced Deoxyribonucleic Acid Polymerase

Infection of HeLa cells with herpes simplex virus leads to a large increase in a new DNA polymerase activity in the nucleus of infected cells. This herpes simplex virus-induced DNA polymerase has been purified 400- to 1300-fold from infected cells and shown to be different in its properties from the normal host cell DNA polymerases. The herpes simplex virus-induced DNA polymerase can be eluted as two peaks of activity on DEAE-cellulose in the presence of glycerol. However, these two DNA polymerase activities seem to have the same molecular weight (1.8 x 105) and exhibit similar properties after further purification on phosphocellulose. The herpes simplex virus-induced DNA polymerase is markedly different from the host DNA polymerases in its high salt requirement for maximal activity. It shows a strong preference for an oligomer-homopolymer template containing deoxyguanylate and deoxycytidylate. A nuclease activity which degrades the polydeoxyadenylate-deoxythymidylate copolymer and the deoxyguanylate-deoxycytidylate homopolymer pair is found to co-chromatograph with the herpes simplex virus-induced DNA polymerase.