A functional interaction of ICP8, the herpes simplex virus single-stranded DNA-binding protein, and the helicase-primase complex that is dependent on the presence of the UL8 subunit
| Autor: | Warren Hurlburt, Daniel J. Tenney, Robert K. Hamatake, Marc Bifano |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
ICP8
DNA polymerase viruses Protein subunit Molecular Sequence Data DNA Primase Herpesvirus 1 Human Single-stranded binding protein Viral Proteins chemistry.chemical_compound Helicase–primase complex Virology Humans Polymerase biology DNA Helicases Processivity biochemical phenomena metabolism and nutrition Molecular biology DNA-Binding Proteins Enzyme Activation Kinetics chemistry biology.protein DNA |
| Zdroj: | Journal of General Virology. 78:857-865 |
| ISSN: | 1465-2099 0022-1317 |
| Popis: | The herpes simplex virus type 1 (HSV) single-stranded DNA-binding protein (SSB, ICP8) stimulates the viral DNA polymerase (Pol) on an oligonucleotide-primed single-stranded DNA template. This stimulation is non-specific since other SSBs also increase Pol activity. However, only ICP8 was stimulatory when Pol activity was dependent upon priming by the viral helicase-primase complex. ICP8 also specifically stimulated the primer synthesis and ATPase activities of the helicase-primase. The mechanism of stimulation was different from that of Pol; helicase-primase stimulation required much lower amounts of ICP8 than the amount that saturates the DNA and optimally stimulates Pol. Furthermore, ICP8 did not act by removing secondary structure as stimulation also occurred on homopolymer templates. While the UL8 component of the helicase-primase is not required for enzymatic activities by a subassembly of the UL5 and UL52 proteins, only the holoenzyme (UL5/8/52) was stimulated by ICP8. These results identify a unique, functional interaction between the ICP8 SSB and the helicase-primase complex, mediated by the UL8 subunit. |
| Databáze: | OpenAIRE |
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