Article
Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter.
Proceedings of the National Academy of Sciences of the United States of America - 4 Jan 2000
Wang L, Grossman S R, Kieff E
Abstract excerpt
The Epstein-Barr virus (EBV) nuclear protein 2 (EBNA2) and herpes simplex virion protein 16 (VP16) acidic domains that mediate transcriptional activation now are found to have affinity for p300, CBP, and PCAF histone acetyltransferases (HATs). Transcriptionally inactive point mutations in these domains lack affinity for p300, CBP, or PCAF. P300 and CBP copurify with the principal HAT activities that bind to EBNA2...
Topics
- Acetyltransferases
- Burkitt Lymphoma
- CREB-Binding Protein
- Cell Cycle Proteins
- DNA-Binding Proteins
- Epstein-Barr Virus Nuclear Antigens
- Fungal Proteins
- Gene Expression Regulation, Viral
- Genes, Reporter
- Herpes Simplex Virus Protein Vmw65
- Herpesvirus 4, Human
- Histone Acetyltransferases