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...
Sparad:
| I publikationen: | J Virol |
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| Huvudupphov: | , , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Utgiven: |
American Society for Microbiology (ASM)
1993
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| Ämnen: | |
| Länkar: | 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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