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Journal of Virology, March 2001, p. 2482-2487, Vol. 75, No. 5
Program in Virology and Departments of
Medicine and Microbiology and Molecular Genetics, Channing Laboratory,
Brigham and Women's Hospital and Harvard University, Boston,
Massachusetts 02115
Received 1 September 2000/Accepted 28 November 2000
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
RBPJ
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.5.2482-2487.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Epstein-Barr Virus Nuclear Protein 2 Has at Least Two N-Terminal
Domains That Mediate Self-Association

binding and acidic activating domains.
*
Corresponding author. Mailing address: Program in
Virology and Departments of Medicine and Microbiology and Molecular
Genetics, Channing Laboratory, Brigham and Women's Hospital and
Harvard University, 181 Longwood Ave., Boston, MA 02115. Phone: (617) 525-4252. Fax: (617) 525-4257. E-mail:
ekieff{at}rics.bwh.harvard.edu.
Present address: Department of Microbiology, St. Marianna
University School of Medicine, Kawasaki 216-8511, Japan.
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