| Literature DB >> 2538835 |
J J Crute1, T Tsurumi, L A Zhu, S K Weller, P D Olivo, M D Challberg, E S Mocarski, I R Lehman.
Abstract
In an earlier report, we described a DNA helicase that is specifically induced upon infection of Vero cells with herpes simplex virus 1. We have purified this enzyme to near homogeneity and found it to consist of three polypeptides with molecular weights of 120,000, 97,000, and 70,000. Immunochemical analysis has shown these polypeptides to be the products of three of the genes UL52, UL5, and UL8 that are required for replication of a plasmid containing a herpes simplex 1 origin (oriS). In addition to helicase activity, the enzyme contains a tightly associated DNA primase. Thus, the three-subunit enzyme is a helicase-primase complex that may prime lagging-strand synthesis as it unwinds DNA at the viral replication fork.Entities:
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Year: 1989 PMID： 2538835 PMCID： PMC286876 DOI： 10.1073/pnas.86.7.2186
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205