Open AccessAssociation of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products.
Author(s) -
Mark S. Dodson,
I Lehman
Publication year - 1991
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.4.1105
Subject(s) - primase , biology , helicase , virology , gene , dna , gene product , microbiology and biotechnology , genetics , polymerase chain reaction , gene expression , reverse transcriptase , rna
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.
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