3' to 5' exonuclease activity of herpes simplex virus type 1 DNA polymerase modulates its strand displacement activity |
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Authors: | Zhu Yali Trego Kelly S Song Liping Parris Deborah S |
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Institution: | Department of Molecular Virology, Immunology, and Medical Genetics, Ohio State University, 333 West Tenth Avenue, Columbus, OH 43210, USA. |
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Abstract: | 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. |
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