Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha
| Autor: | I. R. Lehman, Teresa S.-F. Wang, Sam S. K. Lee, Qun Dong |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1995 |
| Předmět: |
DNA polymerase
Macromolecular Substances DNA polymerase II viruses Enzyme-Linked Immunosorbent Assay Herpesvirus 1 Human Spodoptera Transfection Single-stranded binding protein Cell Line Viral Proteins Replication factor C Animals Humans Replication protein A Multidisciplinary DNA clamp biology DNA replication DNA Polymerase II Molecular biology Recombinant Proteins DNA-Binding Proteins Molecular Weight Kinetics biology.protein Electrophoresis Polyacrylamide Gel Primase Baculoviridae Research Article Protein Binding |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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