Epstein-Barr Virus Immediate-Early Protein BRLF1 Interacts with CBP, Promoting Enhanced BRLF1 Transactivation
Open Access
- 1 July 2001
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 75 (13) , 6228-6234
- https://doi.org/10.1128/jvi.75.13.6228-6234.2001
Abstract
The Epstein-Barr virus (EBV) immediate-early protein BRLF1 is a transcriptional activator that mediates the switch from latent to lytic viral replication. Many transcriptional activators function, in part, due to an interaction with histone acetylases, such as CREB-binding protein (CBP). Here we demonstrate that BRLF1 interacts with the amino and carboxy termini of CBP and that multiple domains of the BRLF1 protein are necessary for this interaction. Furthermore, we show that the interaction between BRLF1 and CBP is important for BRLF1-induced activation of the early lytic EBV gene SM in Raji cells.Keywords
This publication has 87 references indexed in Scilit:
- Inhibition of p53-mediated transactivation and cell cycle arrest by E1A through its p300/CBP-interacting regionSelfcloseTableOncogene, 1997
- The CBP co-activator is a histone acetyltransferaseNature, 1996
- Cooperation of Stat2 and p300/CBP in signalling induced by interferon-αNature, 1996
- A CBP Integrator Complex Mediates Transcriptional Activation and AP-1 Inhibition by Nuclear ReceptorsCell, 1996
- CBP as a transcriptional coactivator of c-Myb.Genes & Development, 1996
- Epstein--Barr virus (EBV) EB1/Zta protein provided in trans and competent for the activation of productive cycle genes does not activate the BZLF1 gene in the EBV genomeJournal of General Virology, 1996
- A family of transcriptional adaptor proteins targeted by the E1A oncoproteinNature, 1995
- Phosphorylated CREB binds specifically to the nuclear protein CBPNature, 1993
- A positive role for histone acetylation in transcription factor access to nucleosomal DNACell, 1993
- Histone acetylation reduces nucleosome core particle linking number changeCell, 1989