Article
Mutations that decrease DNA binding of the processivity factor of the herpes simplex virus DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease the fidelity of DNA replication.
Journal of virology - 1 Apr 2007
Jiang Changying, Hwang Ying T, Randell John C W, Coen Donald M, Hwang Charles B C
Abstract excerpt
The processivity subunit of the herpes simplex virus DNA polymerase, UL42, is essential for viral replication and possesses both Pol- and DNA-binding activities. Previous studies demonstrated that the substitution of alanine for each of four arginine residues, which reside on the positively charged surface of UL42, resulted in decreased DNA binding affinity and a decreased ability to synthesize long-chain DNA by...
Topics
- Animals
- Chlorocebus aethiops
- DNA Replication
- DNA, Recombinant
- DNA, Viral
- DNA-Directed DNA Polymerase
- Exodeoxyribonucleases
- Herpesvirus 1, Human
- Kinetics
- Lac Operon