Direct combinatorial interaction between a herpes simplex virus regulatory protein and a cellular octamer-binding factor mediates specific induction of virus immediate-early gene expression.
We provide evidence for a novel mechanism of transcriptional regulation in which the immediate-early (IE) transactivating protein of herpes simplex virus, Vmw65, is assembled into a specific DNA-binding complex together with a cellular octamer-binding factor (TRF). The assembly of Vmw65/TRF complex requires not only the core TRF recognition site, but also flanking sequences which are dispensable for TRF binding alone. We show from functional analyses that TRF binding by a motif is required but not sufficient to confer induction on a heterologous promoter, and it is the ability of the motif to allow TRF/Vmw65 complex assembly which correlates with functional activity. Thus, for the induction of HSV IE expression, Vmw65 forms a complex with TRF by recognition of the specific subset of appropriately flanked TRF binding sites present in each of the IE genes. This mechanism may provide a paradigm for the selective utilization of the same transcription factor in differential gene expression.
O'Hare
P
P
Marie Curie Research Institute, Surrey, UK.
Goding
C R
CR
Haigh
A
A
D001483:Base Sequence; D004247:DNA / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics*; D005786:Gene Expression Regulation; D015696:Gene Products, tat; D005809:Genes, Regulator; D005814:Genes, Viral; D006801:Humans; D011401:Promoter Regions, Genetic; D000089804:Shelterin Complex; D018139:Simplexvirus / Q000235:genetics* / Q000378:metabolism; D034501:Telomere-Binding Proteins; D014157:Transcription Factors / Q000235:genetics*; D014158:Transcription, Genetic
D004268:DNA-Binding Proteins; D015696:Gene Products, tat; D000089804:Shelterin Complex; C059329:TERF1 protein, human; D034501:Telomere-Binding Proteins; D014157:Transcription Factors; D004247:DNA