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Journal of Virology, September 2003, p. 10147-10153, Vol. 77, No. 18
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.18.10147-10153.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

3' to 5' Exonuclease Activity of Herpes Simplex Virus Type 1 DNA Polymerase Modulates Its Strand Displacement Activity

Yali Zhu,1 Kelly S. Trego,2 Liping Song,1 and Deborah S. Parris1,2*

Department of Molecular Virology, Immunology, and Medical Genetics,1 Department of Molecular Genetics, Ohio State University, Columbus, Ohio 432102

Received 10 March 2003/ Accepted 17 June 2003

Using a minicircle DNA primer-template, the wild-type catalytic subunit of herpes simplex virus type 1 (HSV-1) DNA polymerase (pol) was shown to lack significant strand displacement activity with or without its processivity factor, UL42. However, an exonuclease-deficient (exo-) pol (D368A) was capable of slow strand displacement. Although UL42 increased the rate (2/s) and processivity of strand displacement by exo- pol, the rate was slower than that for gap-filling synthesis. High inherent excision rates on matched primer-templates and rapid idling-turnover (successive rounds of excision and polymerization) of exo-proficient polymerases correlated with poor strand displacement activity. The results suggest that the exo activity of HSV-1 pol modulates its ability to engage in strand displacement, a function that may be important to the viability and genome stability of the virus.

* Corresponding author. Mailing address: Department of Molecular Virology, Immunology, and Medical Genetics, Ohio State University, 2198 Graves Hall, 333 W. Tenth Ave., Columbus, OH 43210. Phone: (614) 292-0735. Fax: (614) 292-9805. E-mail: parris.1{at}osu.edu.

Journal of Virology, September 2003, p. 10147-10153, Vol. 77, No. 18
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.18.10147-10153.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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