Title: Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless.
Abstract: Research Article17 October 1994free access Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless. U. Zimber-Strobl U. Zimber-Strobl Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author L.J. Strobl L.J. Strobl Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author C. Meitinger C. Meitinger Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author R. Hinrichs R. Hinrichs Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author T. Sakai T. Sakai Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author T. Furukawa T. Furukawa Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author T. Honjo T. Honjo Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author G.W. Bornkamm G.W. Bornkamm Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author U. Zimber-Strobl U. Zimber-Strobl Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author L.J. Strobl L.J. Strobl Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author C. Meitinger C. Meitinger Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author R. Hinrichs R. Hinrichs Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author T. Sakai T. Sakai Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author T. Furukawa T. Furukawa Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author T. Honjo T. Honjo Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author G.W. Bornkamm G.W. Bornkamm Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. Search for more papers by this author Author Information U. Zimber-Strobl1, L.J. Strobl1, C. Meitinger1, R. Hinrichs1, T. Sakai1, T. Furukawa1, T. Honjo1 and G.W. Bornkamm1 1Institut für Klinische Molekularbiologie und Tumorgenetik, GSF-Forschungszentrum für Umwelt und Gesundheit, München, Germany. The EMBO Journal (1994)13:4973-4982https://doi.org/10.1002/j.1460-2075.1994.tb06824.x Correction(s) for this article ErratumDecember 1994 PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Epstein-Barr virus nuclear antigen 2 (EBNA-2) plays a crucial role in B cell immortalization by Epstein-Barr virus (EBV), most probably by its ability to transactivate several cellular and viral genes. Recently, we showed that EBNA-2 interacts with the TP1 promoter of EBV through a cellular protein. In this report we provide evidence that this protein is recombination signal binding protein (RBP)-J kappa, highly conserved in evolution, and originally isolated by its ability to bind to the J kappa-type V(D)J recombination signal sequence. To identify the cellular protein interacting with the TP1 promoter, we performed electrophoretic mobility shift assays using binding sequences of known transcription factors, that carry partial homology to the crucial sequences of the EBNA-2 responsive element (EBNA-2RE), as competitor. Competition assays revealed the RBP-J kappa recognition site as a very efficient competitor of cellular TP1 promoter binding protein. In parallel, we purified the protein to homogeneity from Raji cells by two ion-exchange columns and affinity purification using the EBNA-2RE coupled to magnetic beads. Affinity purified fractions separated on SDS-PAGE revealed a single predominant band after silver staining which was recognized by anti-RBP-J kappa monoclonal antibody. These purified fractions exhibited binding specificity for EBNA-2RE and EBNA-2. In vitro-translated murine RBP-2 cDNA reacted with EBNA-2RE and EBNA-2 in the same fashion as the affinity purified protein. The interaction between RBP-J kappa and EBNA-2 is a prerequisite for EBNA-2-mediated transactivation of the TP1 promoter. Previous ArticleNext Article Volume 13Issue 201 October 1994In this issue RelatedDetailsLoading ...