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Article

Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB.

Nucleic acids research - 15 Jun 1996

Gupta R, Emili A, Pan G, Xiao H, Shales M, Greenblatt J, Ingles C J

Abstract excerpt

Contact between a transcriptional activator and one or more components of the RNA polymerase II transcription initiation machinery is generally believed important for activators to function. Several different molecular targets have been suggested for direct contact by herpes simplex virus virion protein VP16, including the general initiation factor TFIIB. In this report we have used several strategies to...

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Identifiers

PMID: 8710503
DOI: 10.1093/nar/24.12.2324
PMCID: PMC145954

Genes

TBP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB.PMID 8710503Read ↗

Structure of the VP16 transactivator target in the Mediator.Semantic proximity Read ↗

Transcriptional activation by DNA-binding derivatives of HSV-1 VP16 that lack the carboxyl-terminal acidic activation domain.Semantic proximity Read ↗

VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection.Semantic proximity Read ↗

Mutational analysis of a transcriptional activation region of the VP16 protein of herpes simplex virus.Semantic proximity Read ↗

NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53.Semantic proximity Read ↗

Defective transcriptional activation by diverse VP16 mutants associated with a common inability to form open promoter complexes.Semantic proximity Read ↗

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.Semantic proximity Read ↗

The H1 and H2 regions of the activation domain of herpes simplex virion protein 16 stimulate transcription through distinct molecular mechanismsSemantic proximity Read ↗

Transcriptional activation by TFIIB mutants that are severely impaired in interaction with promoter DNA and acidic activation domains.Semantic proximity Read ↗

Amino acid substitutions in the herpes simplex virus transactivator VP16 uncouple direct protein-protein interaction and DNA binding from complex assembly and transactivation.Semantic proximity Read ↗

Critical structural elements of the VP16 transcriptional activation domain.Semantic proximity Read ↗

Phosphorylation of the VP16 transcriptional activator protein during herpes simplex virus infection and mutational analysis of putative phosphorylation sites.Semantic proximity Read ↗

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