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Updated: Aug 11, 2026

In situ Subcellular Fractionation of Adherent and Non-adherent Mammalian Cells
Published on: July 23, 2010
Epstein-Barr virus nuclear protein 2 has at least two N-terminal domains that mediate self-association
S Harada1, R Yalamanchili, E Kieff
1Program in Virology and Department of Medicine, Channing Laboratory, Brigham and Women's Hospital and Harvard University, Boston, Massachusetts 02115, USA.
Abstract:
Previous genetic and biochemical analyses have indicated that the Epstein-Barr virus EBNA-2 amino terminus is important for primary B-lymphocyte growth transformation and may be involved in self-association. We now report that EBNA-2 has at least two domains, amino acids 1 to 60 and 96 to 210, which independently mediate homotypic association, 1 to 60 with 1 to 60 and 96 to 210 with 96 to 210. EBNA-2 self-association is likely to be critical to the ability of EBNA-2 to interact simultaneously with multiple cellular transcription factors, coactivators, and histone acetyltransferases through its RBPJkappa binding and acidic activating domains.
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