Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.

We have analyzed the effects of mutations in the herpes simplex virus type 1 DNA polymerase (Pol) C-terminal UL42 binding domain on the activity of Pol and its ability to form complexes with and be stimulated by UL42 in vitro. Wild-type Pol expressed in Saccharomyces cerevisiae was both bound and st...

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Hlavní autoři: Tenney, D J, Micheletti, P A, Stevens, J T, Hamatake, R K, Matthews, J T, Sanchez, A R, Hurlburt, W W, Bifano, M, Cordingley, M G
Médium: Artigo
Jazyk:Inglês
Vydáno: 1993
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Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC237391/
https://ncbi.nlm.nih.gov/pubmed/8380091
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