Abstract
The herpes simplex virus type 2 major DNA-binding protein has been functionally characterized using temperature-sensitive mutants in the complementation group 2-2. The mutants were shown to be defective in the DNA-binding protein gene by mapping the mutants to the area of the genome known to code for the protein, and by demonstrating alterations in the major DNA-binding protein induced in mutant-infected cells. The mutants were shown to be defective in the replication of virus DNA. The nature of this defect was examined by studying virus DNA synthesis in vitro and by the examination of virus enzymes. An effect of mutation in the DNA-binding protein was to destabilize both the DNA polymerase and the alkaline exonuclease.