Cargando…
Polymerase and Exonuclease Activities in Herpes Simplex Virus Type 1 DNA Polymerase Are Not Highly Coordinated
[Image: see text] The herpes polymerase–processivity factor complex consists of the catalytic UL30 subunit containing both polymerase and proofreading exonuclease activities and the UL42 subunit that acts as a processivity factor. Curiously, the highly active exonuclease has minimal impact on the ac...
Autores principales: | Vashishtha, Ashwani Kumar, Kuchta, Robert D. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4303300/ https://www.ncbi.nlm.nih.gov/pubmed/25517265 http://dx.doi.org/10.1021/bi500840v |
Ejemplares similares
-
Assessing the contribution of the herpes simplex virus DNA polymerase to spontaneous mutations
por: Duffy, Karen E, et al.
Publicado: (2002) -
Switching between polymerase and exonuclease sites in DNA polymerase ε
por: Ganai, Rais A., et al.
Publicado: (2015) -
Kinetic Approaches to Understanding the Mechanisms of Fidelity of the Herpes Simplex Virus Type 1 DNA Polymerase
por: Zhu, Yali, et al.
Publicado: (2010) -
Manipulation of RNA polymerase III by Herpes Simplex Virus-1
por: Dremel, Sarah E., et al.
Publicado: (2022) -
Noncanonical prokaryotic X family DNA polymerases lack polymerase activity and act as exonucleases
por: Prostova, Maria, et al.
Publicado: (2022)