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Molecular and Cellular Biology, July 2001, p. 4700-4712, Vol. 21, No. 14
Cold Spring Harbor Laboratory, Cold Spring
Harbor, New York 11724,2 and Graduate
Program in Genetics, State University of New York at Stony Brook,
Stony Brook, New York 117941
Received 6 February 2001/Returned for modification 19 March
2001/Accepted 19 April 2001
Upon infection, the herpes simplex virus (HSV) transcriptional
activator VP16 directs the formation of a multiprotein-DNA complex
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.14.4700-4712.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
DNA Recognition by the Herpes Simplex Virus
Transactivator VP16: a Novel DNA-Binding Structure


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.
*
Corresponding author. Mailing address: Cold Spring
Harbor Laboratory, Cold Spring Harbor, NY 11724. Phone: (516) 367-8401. Fax: (516) 367-8454. E-mail: herr{at}cshl.org.
Present address: Novartis Institute for Biomedical Research,
Summit, NJ 07901.
Present address: DoubleTwist.com, Philadelphia, PA 19104.
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