Article
Mutations within conserved motifs in the 3'-5' exonuclease domain of herpes simplex virus DNA polymerase.
The Journal of general virology - 1 Dec 1995
Hall J D, Orth K L, Sander K L, Swihart B M, Senese R A
Abstract excerpt
We investigated mutations within the presumed 3'-5' exonuclease domain of the DNA polymerase from herpes simplex virus type 1. The mutation sites correspond to residues in DNA polymerase I (Escherichia coli) which bind two metal ions that are required for exonuclease function. To evaluate the eff...
Topics
- Amino Acid Sequence
- Animals
- Cell Line
- Chlorocebus aethiops
- DNA Polymerase I
- DNA, Viral
- DNA-Directed DNA Polymerase
- Enzyme Inhibitors
- Enzyme Stability
- Escherichia coli
- Exodeoxyribonucleases
- Hot Temperature
- Molecular Sequence Data
- Mutation
- Nucleic Acid Synthesis Inhibitors
- Nucleopolyhedroviruses
- Phosphonoacetic Acid
- Plasmids