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.
AUTOR(ES)
O'Hare, P
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=455136Documentos Relacionados
- The TAATGARAT Motif in the Herpes Simplex Virus Immediate-Early Gene Promoters Can Confer both Positive and Negative Responses to Cellular Octamer-Binding Proteins When It Is Located within the Viral Genome
- Construction and characterization of a herpes simplex virus type 1 mutant unable to transinduce immediate-early gene expression.
- Physical interaction between the herpes simplex virus type 1 immediate-early regulatory proteins ICP0 and ICP4.
- Overlapping octamer and TAATGARAT motifs in the VF65-response elements in herpes simplex virus immediate-early promoters represent independent binding sites for cellular nuclear factor III.
- Inhibition of herpes simplex virus type 1 immediate-early gene expression by alpha interferon is not VP16 specific.