Open AccessEpstein-Barr Virus Nuclear Protein 2 Has at Least Two N-Terminal Domains That Mediate Self-Association
Author(s) -
Shizuko Harada,
Ramana Yalamanchili,
Elliott Kieff
Publication year - 2001
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.75.5.2482-2487.2001
Subject(s) - biology , transcription (linguistics) , acetylation , transcription factor , amino acid , histone , virus , dna binding protein , microbiology and biotechnology , histone acetyltransferases , genetics , virology , gene , philosophy , linguistics
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.