Related Experiment Videos
A DNA helicase induced by herpes simplex virus type 1.
J J Crute1, E S Mocarski, I R Lehman
1Department of Biochemistry, Stanford University School of Medicine, CA 94305.
Nucleic Acids Research
|July 25, 1988
Summary
Researchers identified a herpes simplex virus type 1-specific DNA helicase in infected cells. This enzyme may play a crucial role in the replication of the herpes virus genome.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Herpes simplex virus type 1 (HSV-1) infection involves complex viral replication mechanisms.
- Understanding viral enzymes is key to developing antiviral strategies.
Purpose of the Study:
- To identify and characterize enzymes specifically involved in HSV-1 replication.
- To investigate the function of a novel DNA-dependent ATPase found in infected cells.
Main Methods:
- Partial purification of a DNA-dependent ATPase from HSV-1 infected Vero cells.
- Biochemical assays to determine enzyme properties, including molecular weight, substrate specificity, and helicase activity.
- Analysis of enzyme requirements, such as the need for a 3' single-stranded tail.
Main Results:
- A DNA-dependent ATPase, distinct from host enzymes, was identified and partially purified.
- The enzyme exhibits DNA helicase activity, coupling ATP/GTP hydrolysis to DNA unwinding.
- The helicase unwinds DNA in a 5' to 3' direction relative to M13 DNA, requiring a 3' single-stranded tail.
Conclusions:
- The identified enzyme is a herpes-specific DNA helicase.
- This helicase likely functions in the semidiscontinuous replication of the HSV-1 genome, potentially on the lagging strand.