This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kristie, T M Articles by Roizman, B Search for Related Content PubMed PubMed Citation Articles by Kristie, T M Articles by Roizman, B

 Previous Article  |  Next Article 

J Virol. 1988 April; 62(4): 1145-1157

Differentiation and DNA contact points of host proteins binding at the cis site for virion-mediated induction of alpha genes of herpes simplex virus 1.

Marjorie B. Kovler Viral Oncology Laboratories, University of Chicago, Illinois 60637.

ABSTRACT

Transcriptional trans-activation of the five herpes simplex virus 1 alpha genes by the alpha trans-inducing factor requires a cis-acting site (alpha TIC; with the consensus 5'-GyATGnTAATGArATTCyTTGnGGG-3') located in the promoter-regulatory domains of the alpha genes. In DNA band shift assays with nuclear extracts from either mock-infected or infected cells, the DNA fragments containing an alpha TIC sequence from the alpha 0, alpha 4, and alpha 27 genes formed several cellular protein-DNA complexes designated alpha H1, alpha H2, and alpha H3. The host proteins that formed the alpha H2 and alpha H3 complexes were differentiated from those that formed the alpha H1 complex but not from each other by chromatography and specificity of the DNA-binding sites. The alpha H1 proteins protected the alpha TIC sequence of all three genes from DNase I digestion. Methylation of the purines in the sequence 5'-GyATGnTAAT-3' located at the 5' terminus of the alpha TIC sites precluded the binding of alpha H1. The binding site of the alpha H2-alpha H3 proteins in the alpha 27 gene alpha TIC overlapped, in part, with the alpha H1-binding site. The binding of these proteins was precluded by methylation of the purine residues in the sequence 5'-GCCACGTG-3' located at the 3' terminus of the DNase I footprint. The maximum apparent molecular weight of alpha H1 was 110,000, whereas that of alpha H2-alpha H3 was 64,000. A protein designated alpha H2', resembling alpha H2-alpha H3 with respect to molecular weight and chromatographic properties but differing in sequence specificity, bound to a site adjacent to the alpha H1 site in the fragment carrying an alpha TIC sequence of the alpha 4 gene. alpha H1 and alpha H2-alpha H3 or alpha H2' bound concurrently, notwithstanding the apparent overlap in the DNase I footprints.

This article has been cited by other articles:

• Carroll, K. D., Khadim, F., Spadavecchia, S., Palmeri, D., Lukac, D. M. (2007). Direct Interactions of Kaposi's Sarcoma-Associated Herpesvirus/Human Herpesvirus 8 ORF50/Rta Protein with the Cellular Protein Octamer-1 and DNA Are Critical for Specifying Transactivation of a Delayed-Early Promoter and Stimulating Viral Reactivation. J. Virol. 81: 8451-8467 [Abstract] [Full Text]  
• Jones, C. (2003). Herpes Simplex Virus Type 1 and Bovine Herpesvirus 1 Latency. Clin. Microbiol. Rev. 16: 79-95 [Abstract] [Full Text]  
• Preston, C. M. (2000). Repression of viral transcription during herpes simplex virus latency. J. Gen. Virol. 81: 1-19 [Full Text]  
• Kristie, T. M. (1997). The Mouse Homologue of the Human Transcription Factor C1 (Host Cell Factor). CONSERVATION OF FORMS AND FUNCTION. J. Biol. Chem. 272: 26749-26755 [Abstract] [Full Text]  
• Kristie, T. M., Pomerantz, J. L., Twomey, T. C., Parent, S. A., Sharp, P. A. (1995). The Cellular C1 Factor of the Herpes Simplex Virus Enhancer Complex Is a Family of Polypeptides. J. Biol. Chem. 270: 4387-4394 [Abstract] [Full Text]  
• Kristie, T M, Sharp, P A (1990). Interactions of the Oct-1 POU subdomains with specific DNA sequences and with the HSV alpha-trans-activator protein.. Genes Dev. 4: 2383-2396 [Abstract]  
• LeBowitz, J H, Clerc, R G, Brenowitz, M, Sharp, P A (1989). The Oct-2 protein binds cooperatively to adjacent octamer sites.. Genes Dev. 3: 1625-1638 [Abstract]  
• LaMarco, K L, McKnight, S L (1989). Purification of a set of cellular polypeptides that bind to the purine-rich cis-regulatory element of herpes simplex virus immediate early genes.. Genes Dev. 3: 1372-1383 [Abstract]