@article{mbs:/content/journal/jgv/10.1099/0022-1317-79-2-363, author = "Bourillot, Pierre-Yves and Waltzer, Lucas and Sergeant, Alain and Manet, Evelyne", title = "Transcriptional repression by the Epstein-Barr virus EBNA3A protein tethered to DNA does not require RBP-Jkappa", journal= "Journal of General Virology", year = "1998", volume = "79", number = "2", pages = "363-370", doi = "https://doi.org/10.1099/0022-1317-79-2-363", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-79-2-363", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The Epstein-Barr virus (EBV) proteins EBNA1, EBNA2, EBNA3A, EBNA3C, LMP1 and EBNA-LP are essential for the in vitro immortalization of primary B lymphocytes by EBV. EBNA2 is a transcriptional activator of viral and cellular genes. Both EBNA3A and EBNA3C have been shown to specifically inhibit EBNA2-activated transcription by direct interaction with RBP-J k , a cellular DNA-binding factor known to recruit EBNA2 to EBNA2-responsive genes. This interaction interferes with the binding of RBP-J k to DNA in vitro, and this is probably the mechanism by which EBNA3A and EBNA3C repress EBNA2-acti- vated transcription in vivo. EBNA3A and EBNA3C also directly repress transcription when tethered to a promoter via the DNA-binding domain of the yeast Gal4 protein. As RBP-J k has been previously shown to be a repressor in mammalian cells, this repression could be due to the recruitment of RBP-J k by Gal4-EBNA3A and 3C. In this study, we have precisely mapped the domain of EBNA3A involved in the interaction with RBP-J k and we have shown that interaction with RBP-J k is not required for the Gal4-EBNA3A-mediated repression. Furthermore, we have characterized in EBNA3A a domain of 143 amino acids which is necessary and sufficient for EBNA3A-dependent repression.", }