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Article

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

Virology - 10 May 1995

Popova B, Bilan P, Xiao P, Faught M, Capone J P

Abstract excerpt

The herpes simplex virus transactivator VP16 directs the assembly of a multicomponent protein-DNA complex with cellular components Oct-1 and VCAF-1, contributing a potent carboxyl-terminal acidic activation domain that is essential for activation of gene expression in mammalian cells. We show here that VP16, devoid of this acidic activation domain, functions as a strong transcriptional activator in the yeast...

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Identifiers

PMID: 7747469
DOI: 10.1006/viro.1995.1227

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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→

Click a neighbor to travelStep 1 · 12 closest

Transcriptional activation by DNA-binding derivatives of HSV-1 VP16 that lack the carboxyl-terminal acidic activation domain.PMID 7747469Read ↗

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

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

The herpes simplex virus trans-activator VP16 recognizes the Oct-1 homeo domain: evidence for a homeo domain recognition subdomain.Semantic proximity Read ↗

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

Host factors associated with either VP16 or VP16‐induced complex differentially affect HSV‐1 lytic infectionSemantic proximity Read ↗

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

The Herpesvirus Transactivator VP16 Mimics a Human Basic Domain Leucine Zipper Protein, Luman, in Its Interaction with HCFSemantic 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 ↗

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

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

Deletion of the VP16 open reading frame of herpes simplex virus type 1.Semantic proximity Read ↗

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