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The cellular factor Oct-1 is selectively recruited, together with at least one other cellular protein (CFF), into a multicomponent transcription complex whose assembly is directed by the herpes simplex virus regulatory protein Vmw65 (VP16). The acidic carboxy terminus of Vmw65 is not involved in assembly of the complex but is absolutely required for subsequent transcriptional activation. Elucidation of the mechanism of action of Vmw65 is important for an understanding not only of combinatorial control of gene expression by POU- and homeodomain proteins but also of the interaction(s) between activation domains of regulatory proteins and components of the basal transcriptional apparatus. We used a combination of limited proteolysis with a number of site-specific proteases and immunological detection to demonstrate the presence of two main surface-exposed regions in Vmw65. We mapped these sites to within a few amino acids at positions 365-370 408/409. The site at 408/409 is indicative of a flexible exposed linker region between the acidic carboxy-terminal activation domain (residues 430-480) and an N-terminal domain involved in complex formation with the two cellular factors. The site around residues 365-370 is precisely within a region that results from this and other laboratories have shown to be critical for complex formation. Furthermore, we show that this site is selectively protected from proteolysis after complex assembly. Finally, using a series of overlapping peptide encompassing this region, we show that the eight amino acids, R-E-H-A-Y-S-R-A, from positions 360 through 367 are sufficient to inhibit complex formation by intact Vmw65. We propose that these residues contain sufficient information to selectively bind one of the cellular partners involved in complex assembly and that these residues are located in a physical surface-exposed domain of the protein.

Mapping of a major surface-exposed site in herpes simplex virus protein Vmw65 to a region of direct interaction in a transcription complex assembly