DNA Recognition by the Herpes Simplex Virus Transactivator VP16: a Novel DNA-Binding Structure
Open Access
- 1 July 2001
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 21 (14) , 4700-4712
- https://doi.org/10.1128/mcb.21.14.4700-4712.2001
Abstract
Upon infection, the herpes simplex virus (HSV) transcriptional activator VP16 directs the formation of a multiprotein-DNA complex—the VP16-induced complex—with two cellular proteins, the host cell factor HCF-1 and the POU domain transcription factor Oct-1, on TAATGARAT-containing sequences found in the promoters of HSV immediate-early genes. HSV VP16 contains carboxy-terminal sequences important for transcriptional activation and a central conserved core that is important for VP16-induced complex assembly. On its own, VP16 displays little, if any, sequence-specific DNA-binding activity. We show here that, within the VP16-induced complex, however, the VP16 core has an important role in DNA binding. Mutation of basic residues on the surface of the VP16 core reveals a novel DNA-binding surface with essential residues which are conserved among VP16 orthologs. These results illuminate how, through association with DNA, VP16 is able to interpret cis-regulatory signals in the DNA to direct the assembly of a multiprotein-DNA transcriptional regulatory complex.Keywords
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