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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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Publicado no:J Virol
Principais autores: 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
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Microbiology (ASM) 1993
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC237391/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8380091/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.67.1.543-547.1993
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