1887

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-Trp-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.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-77-5-991
1996-05-01
2019-11-21
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-77-5-991
Loading

Most Cited This Month

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error