Herpes Simplex Virus Type 1 DNA Polymerase: Eukaryotic Model Enzyme and Principal Target of Antiviral Therapy

Author(s):  
Charles W. Knopf ◽  
Reiner Strick
2013 ◽  
Vol 207 (8) ◽  
pp. 1295-1305 ◽  
Author(s):  
Graciela Andrei ◽  
Aspasia Georgala ◽  
Dimitri Topalis ◽  
Pierre Fiten ◽  
Michel Aoun ◽  
...  

1994 ◽  
Vol 75 (11) ◽  
pp. 3127-3135 ◽  
Author(s):  
H. S. Marsden ◽  
M. Murphy ◽  
G. L. McVey ◽  
K. A. MacEachran ◽  
A. M. Owsianka ◽  
...  

FEBS Letters ◽  
1981 ◽  
Vol 126 (2) ◽  
pp. 157-160 ◽  
Author(s):  
Heather M. Wallace ◽  
Herbert N. Baybutt ◽  
Colin K. Pearson ◽  
Hamish M. Keir

2003 ◽  
Vol 77 (18) ◽  
pp. 10147-10153 ◽  
Author(s):  
Yali Zhu ◽  
Kelly S. Trego ◽  
Liping Song ◽  
Deborah S. Parris

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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