| Literature DB >> 1847509 |
Abstract
Herpes simplex virus 1 encodes a helicase-primase that is composed of the products of the UL5, UL8, and UL52 genes. A stable subassembly consisting of only the UL5 and UL52 gene products has been purified to near homogeneity from insect cells doubly infected with baculovirus recombinant for these two genes. The purified subassembly has the DNA-dependent ATPase, DNA-dependent GTPase, DNA helicase, and DNA primase activities that are characteristic of the three-subunit holoenzyme. The purified UL8 gene product, although required for viral DNA replication, neither exhibits these enzymatic activities nor stably associates with either the UL5 or the UL52 gene product.Entities:
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Year: 1991 PMID: 1847509 PMCID: PMC50965 DOI: 10.1073/pnas.88.4.1105
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205