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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.
Author(s) -
O'Hare P.,
Goding C. R.,
Haigh A.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03320.x
Subject(s) - marie curie , histone octamer , biology , binding site , virus , herpes simplex virus , microbiology and biotechnology , gene , virology , genetics , histone , european union , business , economic policy , nucleosome
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.