Epstein-Barr virus immediate-early protein BRLF1 interacts with CBP, promoting enhanced BRLF1 transactivation.
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.
Swenson
J J
JJ
Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599, USA.
Holley-Guthrie
E
E
Kenney
S C
SC
D050882:CREB-Binding Protein; D004268:DNA-Binding Proteins / Q000502:physiology; D006367:HeLa Cells; D004854:Herpesvirus 4, Human / Q000235:genetics; D006801:Humans; D017874:Immediate-Early Proteins / Q000502:physiology*; D009687:Nuclear Proteins / Q000502:physiology*; D010750:Phosphoproteins / Q000235:genetics; D011401:Promoter Regions, Genetic; D015534:Trans-Activators / Q000235:genetics / Q000502:physiology*; D015533:Transcriptional Activation; D014764:Viral Proteins
C068382:BRLF1 protein, Human herpesvirus 4; C063676:BZLF1 protein, Herpesvirus 4, Human; D004268:DNA-Binding Proteins; D017874:Immediate-Early Proteins; D009687:Nuclear Proteins; D010750:Phosphoproteins; C090236:SM protein, Human herpesvirus 4; D015534:Trans-Activators; D014764:Viral Proteins; D050882:CREB-Binding Protein; C494363:CREBBP protein, human