Herpes simplex virus non-structural proteins. III. Function of the major DNA-binding protein.
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.
D004265:DNA Helicases / Q000235:genetics*; D004279:DNA, Viral / Q000096:biosynthesis; D004268:DNA-Binding Proteins; D004259:DNA-Directed DNA Polymerase / Q000096:biosynthesis; D003673:Defective Viruses / Q000235:genetics; D004790:Enzyme Induction; D005090:Exodeoxyribonucleases / Q000096:biosynthesis; D005814:Genes, Viral; D005816:Genetic Complementation Test; D005819:Genetic Markers; D009154:Mutation; D018139:Simplexvirus / Q000235:genetics*; D013696:Temperature
D004279:DNA, Viral; D004268:DNA-Binding Proteins; D005819:Genetic Markers; D004259:DNA-Directed DNA Polymerase; D005090:Exodeoxyribonucleases; D004265:DNA Helicases