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Nucleic Acids Research, 1988, Vol. 16, No. 14 6585-6596
© 1988

Articles

A DNA helicase induced by herpes simplex virus type 1

James J. Crute, Edward S. Mocarski1 and I.R. Lehman

Departments of Biochemistry, Stanford University School of Medicine Stanford, CA 94305, USA 1Departments of Medical Microbiology, Stanford University School of Medicine Stanford, CA 94305, USA

Received March 28, 1988. 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.


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