Evidence of DNA: protein interactions that mediate HSV-1 immediate early gene activation by VP16.

S. J. Triezenberg, K. L. LaMarco, S. L. McKnight

Research output: Contribution to journalArticle

169 Citations (Scopus)

Abstract

The viral genes first expressed upon lytic infection by herpes simplex virus type 1 (HSV-1) encode the five immediate early (IE) proteins. IE gene expression is potently and specifically induced by a virion protein termed VP16. Previous studies have shown that the activating properties of VP16 are IE gene specific and mediated by upstream regulatory elements common to each IE gene. Paradoxically, however, VP16 does not appear to be a sequence-specific DNA-binding protein. To understand the specificity of VP16 activation, we identified the cis-regulatory sequences of an IE gene that mediate VP16 response. Two distinct DNA sequence motifs enable the ICP4 gene to respond to VP16. Biochemical fractionation of nuclear proteins from uninfected cells revealed the existence of cellular proteins that bind directly to each of these VP16 cis-response elements. These observations, in concert with the identification of functional domains of the VP16 protein, lead to the hypothesis that VP16 achieves activation specificity via protein: protein, rather than protein: DNA, interactions.

Original languageEnglish (US)
Pages (from-to)730-742
Number of pages13
JournalGenes & development
Volume2
Issue number6
StatePublished - Jun 1988

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Immediate-Early Genes
Human Herpesvirus 1
Transcriptional Activation
Herpes Simplex Virus Protein Vmw65
DNA
Proteins
Immediate-Early Proteins
Nucleotide Motifs
Viral Genes
DNA-Binding Proteins
Response Elements
Nuclear Proteins
Virion
Gene Expression
Infection
Genes

ASJC Scopus subject areas

  • Developmental Biology
  • Genetics

Cite this

Evidence of DNA : protein interactions that mediate HSV-1 immediate early gene activation by VP16. / Triezenberg, S. J.; LaMarco, K. L.; McKnight, S. L.

In: Genes & development, Vol. 2, No. 6, 06.1988, p. 730-742.

Research output: Contribution to journalArticle

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