HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Sauder, C. Articles by Grässer, F. A. Search for Related Content PubMed PubMed Citation Articles by Sauder, C. Articles by Grässer, F. A. Agricola Articles by Sauder, C. Articles by Grässer, F. A.

Mutational analysis of the Epstein—Barr virus nuclear antigen 2 by far-Western blotting and DNA-binding studies

¹ Institut für medizinische Mikrobiologie und Hygiene der Universitätskliniken des Saarlandes, Abteilung Virologie, Haus 47, 66421 Homburg/Saar, Germany,
² Department of Medicine, University of Washington and Veterans Administration Medical Center, Seattle, Washington, USA,
³ Division of Oncology, Department of Medicine, HSC T-17, 080, State University of New York Stony Brook, NY 11790-8174, USA,
⁴ Institut für Immunologie, Hämatologikum, GSF, Marchioninistrasse 25, 81377 München, Germany
and⁵ Institut für Klinische Molekularbiologie und Tumorgenetik, Hämatologikum, GSF, Marchioninistrasse 25, 81377 München, Germany

We have previously shown by far-Western blotting that the Epstein—Barr virus nuclear antigen 2 (EBNA-2) both binds to a cellular protein of 130 kDa and histone H1, with the complex between EBNA-2 and p130 being tighter than between EBNA-2 and histone H1. Here we demonstrate that the N terminus of EBNA-2, which was previously shown to be necessary for transformation of B lymphocytes by EBNA-2, is essential for binding to p130. We further show data indicating that the binding of EBNA-2 to histone H1 appears not to be mediated exclusively via the basic Arg-Gly rich region in the C-terminal part of EBNA-2. With a MAb directed against the Trp-Trp³²²-Pro (WWP) motif of EBNA-2, which is known to be essential for the interaction of EBNA-2 with the cellular factor RBPJ/CBF1, we could inhibit the DNA binding of EBNA-2, providing further evidence that this region of EBNA-2 forms direct contact with RBPJ/CBF1.

^* Author for correspondence. Fax +49 6841 16 3980. e-mail graesser@med-rz.uni-sb.de

Received 27 September 1995; accepted 19 December 1995.

This article has been cited by other articles:

				M. D. Voss, A. Hille, S. Barth, A. Spurk, F. Hennrich, D. Holzer, N. Mueller-Lantzsch, E. Kremmer, and F. A. Grasser Functional Cooperation of Epstein-Barr Virus Nuclear Antigen 2 and the Survival Motor Neuron Protein in Transactivation of the Viral LMP1 Promoter J. Virol., December 1, 2001; 75(23): 11781 - 11790. [Abstract] [Full Text]