kinetic approaches to understanding the mechanisms of fidelity of the herpes simplex virus type 1 dna polymerase
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ID: 147298
2010
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Abstract
We discuss how the results of presteady-state and steady-state kinetic analysis of the polymerizing and excision activities of herpes simplex virus type 1 (HSV-1) DNA polymerase have led to a better understanding of the mechanisms controlling fidelity of this important model replication polymerase. Despite a poorer misincorporation frequency compared to other replicative polymerases with intrinsic 3′ to 5′ exonuclease (exo) activity, HSV-1 DNA replication fidelity is enhanced by a high kinetic barrier to extending a primer/template containing a mismatch or abasic lesion and by the dynamic ability of the polymerase to switch the primer terminus between the exo and polymerizing active sites. The HSV-1 polymerase with a catalytically inactivated exo activity possesses reduced rates of primer switching and fails to support productive replication, suggesting a novel means to target polymerase for replication inhibition.
| Reference Key |
zhu2010journalkinetic
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|---|---|
| Authors | ;Yali Zhu;Jason Stroud;Liping Song;Deborah S. Parris |
| Journal | gas separation \& purification |
| Year | 2010 |
| DOI |
10.4061/2010/631595
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| URL | |
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