Open AccessHerpes simplex virus 1 helicase-primase: a complex of three herpes-encoded gene products.
Author(s) -
James J. Crute,
Tatsuya Tsurumi,
Liang Zhu,
Sandra K. Weller,
Paul D. Olivo,
M D Challberg,
Edward S. Mocarski,
I Lehman
Publication year - 1989
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.86.7.2186
Subject(s) - primase , helicase , biology , herpes simplex virus , virology , single stranded binding protein , prokaryotic dna replication , gene , dna , microbiology and biotechnology , plasmid , rna helicase a , dna replication , virus , genetics , origin of replication , polymerase chain reaction , rna , dna binding protein , reverse transcriptase , transcription factor
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.
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