Abstract
The herpes simplex virus alpha, or immediate early, protein ICP4 has been shown to be central to the control of the early stages of virus replication. The detailed mechanism of this control is unknown. In this communication we show that purified ICP4 was unable to bind to DNA even though the protein was capable of such activity in a crude extract. Addition of either infected- or uninfected-cell extracts to the purified protein restored its DNA-binding activity. These results suggest that ICP4 binds to DNA only via a component of uninfected cells.
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- Bookout J. B., Levy C. C. Comparative examination of the polypeptides of herpes simplex virus: types 1 and 2. Virology. 1980 Feb;101(1):198–216. doi: 10.1016/0042-6822(80)90496-1. [DOI] [PubMed] [Google Scholar]
- Courtney R. J., Powell K. L. Immunological and biochemical characterization of polypeptides induced by herpes simplex virus types 1 and 2. IARC Sci Publ. 1975;(11 Pt 1):63–73. [PubMed] [Google Scholar]
- Dixon R. A., Schaffer P. A. Fine-structure mapping and functional analysis of temperature-sensitive mutants in the gene encoding the herpes simplex virus type 1 immediate early protein VP175. J Virol. 1980 Oct;36(1):189–203. doi: 10.1128/jvi.36.1.189-203.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Halliburton I. W. Intertypic recombinants of herpes simplex viruses. J Gen Virol. 1980 May;48(1):1–23. doi: 10.1099/0022-1317-48-1-1. [DOI] [PubMed] [Google Scholar]
- Hay R. T., Hay J. Properties of herpesvirus-induced "immediate early" polypeptides. Virology. 1980 Jul 15;104(1):230–234. doi: 10.1016/0042-6822(80)90381-5. [DOI] [PubMed] [Google Scholar]
- Honess R. W., Roizman B. Regulation of herpesvirus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins. J Virol. 1974 Jul;14(1):8–19. doi: 10.1128/jvi.14.1.8-19.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Minson A., Bell S. E., Bastow K. Correlation of the virus sequence content and biological properties of cells carrying the herpes simplex virus type 2 thymidine kinase gene. J Gen Virol. 1982 Jan;58(Pt 1):127–138. doi: 10.1099/0022-1317-58-1-127. [DOI] [PubMed] [Google Scholar]
- Powell K. L., Courtney R. J. Polypeptide synthesized in herpes simplex virus type 2-infected HEp-2 cells. Virology. 1975 Jul;66(1):217–228. doi: 10.1016/0042-6822(75)90192-0. [DOI] [PubMed] [Google Scholar]
- Powell K. L., Purifoy D. J. Nonstructural proteins of herpes simplex virus. I. Purification of the induced DNA polymerase. J Virol. 1977 Nov;24(2):618–626. doi: 10.1128/jvi.24.2.618-626.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Preston C. M. Control of herpes simplex virus type 1 mRNA synthesis in cells infected with wild-type virus or the temperature-sensitive mutant tsK. J Virol. 1979 Jan;29(1):275–284. doi: 10.1128/jvi.29.1.275-284.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Preston V. G. Fine-structure mapping of herpes simplex virus type 1 temperature-sensitive mutations within the short repeat region of the genome. J Virol. 1981 Jul;39(1):150–161. doi: 10.1128/jvi.39.1.150-161.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Purifoy D. J., Powell K. L. DNA-binding proteins induced by herpes simplex virus type 2 in HEp-2 cells. J Virol. 1976 Aug;19(2):717–731. doi: 10.1128/jvi.19.2.717-731.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wilcox K. W., Kohn A., Sklyanskaya E., Roizman B. Herpes simplex virus phosphoproteins. I. Phosphate cycles on and off some viral polypeptides and can alter their affinity for DNA. J Virol. 1980 Jan;33(1):167–182. doi: 10.1128/jvi.33.1.167-182.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]