A Herpesvirus Trans-Activating Protein Interacts with Transcription Factor OTF-1 and Other Cellular Proteins

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 85; no. 17; pp. 6347 - 6351
• Main Authors: Gerster, Thomas, Roeder, Robert G.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01.09.1988; National Acad Sciences
• Subjects: Base Sequence; Biological and medical sciences; DNA; DNA, Viral - metabolism; Fundamental and applied biological sciences. Psychology; Gene Products, tat; Genes; Genes, Viral; HeLa cells; HeLa Cells - metabolism; Human herpesvirus 1; Humans; Immediate early genes; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Nuclear Proteins - metabolism; Oligodeoxyribonucleotides; Oligonucleotide probes; Oligonucleotides; Oncogene Proteins, Viral - metabolism; Protein Biosynthesis; Reticulocytes; RNA; Simplexvirus - genetics; Transcription factors; Transcription Factors - metabolism; Transcription. Transcription factor. Splicing. Rna processing; Viruses; Virus; Regulation(control); Transcription; Herpesviridae; Alphaherpesvirinae; Trans acting regulatory factor; Molecular interaction
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.85.17.6347

Immediate early genes of herpes simplex viruses contain one or more copies of the conserved TAAT-GARAT (where R is purine) DNA motif. A virus-encoded regulatory protein (Vmw65) is believed to stimulate transcription via this element, although the protein does not bind directly to DNA. Overlapping the TAATGARAT element in many cases is an octamer sequence (ATGCAAAT) that is involved both in transcription by RNA polymerases II and III and in adenovirus DNA replication. So far at least two proteins (OTF-1 and OTF-2) have been identified that bind to the octamer. We show that both affinity-purified OTF-1 and OTF-2 bind to the TAATGARAT sequence and that Vmw65 induces the formation of an additional complex that involves OTF-1 and that is further retarded in a band-shift gel assay. Complementation experiments involving addition of purified OTF-1 to nuclear extracts that have been depleted of endogenous OTF-1 show that at least one other cellular factor(s) is required for complex formation. This cellular factor may be involved in recognition of the GARAT sequence.