Evidence that the nuclease activities associated with the herpes simplex type 1 DNA polymerase are due to the 3'-5' exonuclease.
We investigated nuclease activities associated with the catalytic subunit of herpes simplex virus type 1 DNA polymerase. We confirm that a 3'-5' exonuclease copurifies with this enzyme. Previous reports suggested that a 5' DNase was intrinsic to the polymerase. Our preparation lacks such activity.
Hall
J D
JD
Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721, USA.
Orth
K L
KL
Claus-Walker
D
D
D000818:Animals; D002460:Cell Line; D004259:DNA-Directed DNA Polymerase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D043211:Exodeoxyribonuclease V; D005090:Exodeoxyribonucleases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D018259:Herpesvirus 1, Human / Q000201:enzymology*; D006801:Humans; D009154:Mutation; D018411:Spodoptera / Q000166:cytology; D013379:Substrate Specificity; D014764:Viral Proteins
D014764:Viral Proteins; D004259:DNA-Directed DNA Polymerase; D005090:Exodeoxyribonucleases; C043417:DNA polymerase, Simplexvirus; D043211:Exodeoxyribonuclease V