Abstract
The herpes simplex virus 1 (HSV-1) genome encodes seven polypeptides that are required for its replication. These include a heterodimeric DNA polymerase, a single-strand-DNA-binding protein, a heterotrimeric helicase/primase, and a protein (UL9 protein) that binds specifically to an HSV-1 origin of replication (oris). We demonstrate here that UL9 protein interacts specifically with the 180-kDa catalytic subunit of the cellular DNA polymerase alpha-primase. This interaction can be detected by immunoprecipitation with antibodies directed against either of these proteins, by gel mobility shift of an oris-UL9 protein complex, and by stimulation of DNA polymerase activity by the UL9 protein. These findings suggest that enzymes required for cellular DNA replication also participate in HSV-1 DNA replication.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Baculoviridae
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Cell Line
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DNA Polymerase II / biosynthesis
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DNA Polymerase II / isolation & purification
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DNA Polymerase II / metabolism*
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DNA-Binding Proteins / biosynthesis
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DNA-Binding Proteins / isolation & purification
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DNA-Binding Proteins / metabolism*
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Electrophoresis, Polyacrylamide Gel
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Enzyme-Linked Immunosorbent Assay
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Herpesvirus 1, Human / genetics
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Herpesvirus 1, Human / metabolism*
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Humans
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Kinetics
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Macromolecular Substances
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Molecular Weight
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Protein Binding
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Spodoptera
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Transfection
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Viral Proteins / biosynthesis
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Viral Proteins / isolation & purification
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Viral Proteins / metabolism*
Substances
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DNA-Binding Proteins
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Macromolecular Substances
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Recombinant Proteins
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Viral Proteins
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origin-binding proteins, viral
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UL9 protein, Human herpesvirus 1
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DNA Polymerase II