Activities of heterodimers composed of DNA-binding- and transactivation-deficient subunits of the herpes simplex virus regulatory protein ICP4.

doi:10.1128/JVI.65.1.299-307.1991

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Article

Activities of heterodimers composed of DNA-binding- and transactivation-deficient subunits of the herpes simplex virus regulatory protein ICP4.

Journal of virology - 1 Jan 1991

Shepard A A, DeLuca N A

Abstract excerpt

Two mutant strains (vi12 and vi13) of herpes simplex virus that contain insertion mutations in the sequences that encode the DNA-binding domain of viral regulatory protein ICP4 were generated. Both mutations disrupted specific DNA binding and resulted in transcriptionally inactive molecules; however, the ability of the mutant proteins to form dimers was retained. The mutant proteins formed heterodimers with an...

Topics

Animals
Blotting, Northern
DNA Replication
DNA, Viral
DNA-Binding Proteins
Genetic Complementation Test
Genotype
Immediate-Early Proteins
Macromolecular Substances
Mutagenesis, Insertional
Nucleic Acid Hybridization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Plasmids

RNA, Messenger

Simplexvirus

Transcriptional Activation

Vero Cells

Viral Proteins

Viral Regulatory and Accessory Proteins

Source

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Identifiers

PMID: 1845890
DOI: 10.1128/JVI.65.1.299-307.1991
PMCID: PMC240517

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1845890-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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