The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.

The herpes simplex virus DNA polymerase is composed of two subunits, a large catalytic subunit (Pol) and a smaller subunit (UL42) that increases the processivity of the holoenzyme. The interaction between the two polypeptides is of interest both for the mechanism by which it enables the enzyme to sy...

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Foilsithe in:J Virol
Main Authors: Digard, P, Bebrin, W R, Weisshart, K, Coen, D M
Formáid: Artigo
Teanga:Inglês
Foilsithe: American Society for Microbiology (ASM) 1993
Ábhair:
Research Article
Rochtain Ar Líne:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC237376/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8380085/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.67.1.398-406.1993
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