A DNA helicase induced by herpes simplex virus type 1.
We have identified and partially purified a DNA-dependent ATPase that is present specifically in herpes simplex virus type 1-infected Vero cells. The enzyme which has a molecular weight of approximately 440,000 differs from the comparable host enzyme in its elution from phosphocellulose columns and in its nucleoside triphosphate specificity. The partially purified DNA-dependent ATPase is also a DNA helicase that couples ATP or GTP hydrolysis to the displacement of an oligonucleotide annealed to M13 single-stranded DNA. The enzyme requires a 3' single-stranded tail on the duplex substrate, suggesting that the polarity of unwinding is 5'----3' relative to the M13 DNA. The herpes specific DNA helicase may therefore translocate on the lagging strand in the semidiscontinuous replication of the herpes virus 1 genome.
Crute
J J
JJ
Department of Biochemistry, Stanford University School of Medicine, CA 94305.
Mocarski
E S
ES
Lehman
I R
IR
D000251:Adenosine Triphosphatases / Q000096:biosynthesis* / Q000302:isolation & purification; D000818:Animals; D004265:DNA Helicases / Q000096:biosynthesis* / Q000302:isolation & purification; D004790:Enzyme Induction; D007700:Kinetics; D018139:Simplexvirus / Q000502:physiology*; D013379:Substrate Specificity; D014709:Vero Cells
D000251:Adenosine Triphosphatases; D004265:DNA Helicases