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Article

Analysis of the varicella-zoster virus IE62 N-terminal acidic transactivating domain and its interaction with the human mediator complex.

Journal of virology - 1 Jun 2009

Yamamoto Shinobu, Eletsky Alexander, Szyperski Thomas, Hay John, Ruyechan William T

Abstract excerpt

The varicella-zoster virus major transactivator, IE62, contains a potent N-terminal acidic transcriptional activation domain (TAD). Our experiments revealed that the minimal IE62 TAD encompasses amino acids (aa) 19 to 67. We showed that the minimal TAD interacts with the human Mediator complex. Site-specific mutations revealed residues throughout the minimal TAD that are important for both activation and Mediator...

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Share to Herpesvirus 3, Human
Share to Immediate-Early Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mediator Complex

Share to Mutagenesis, Site-Directed

Share to Protein Structure, Secondary

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Source

Open in PubMed Open full text

Identifiers

PMID: 19357160
DOI: 10.1128/JVI.00054-09
PMCID: PMC2687382

Genes

MED25

Provenance

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.

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