May 1, 1996

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

The Journal of General Virology
C SauderFriedrich A Grässer

Abstract

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 RBPJkappa/CBF1, we could inhibit the DNA binding of EBNA-2, providing further evidence that this region of EBNA-2 forms direct contact with RBPJkappa/CBF1.

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Mentioned in this Paper

Carboxy-Terminal Amino Acid
Structure-Activity Relationship
NOLC1 gene
RBL2 wt Allele
RBL2 protein, human
RBPJ gene
B-Lymphocytes
RBPJ
Western Blot
Histone H1

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