Epstein-Barr virus nuclear protein 2 has at least two N-terminal domains that mediate self-association.
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.
Harada
S
S
Program in Virology and Department of Medicine, Channing Laboratory, Brigham and Women's Hospital and Harvard University, Boston, Massachusetts 02115, USA.
Yalamanchili
R
R
Kieff
E
E
D000596:Amino Acids / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D019309:Epstein-Barr Virus Nuclear Antigens / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017353:Gene Deletion; D011233:Precipitin Tests; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014162:Transfection; D014764:Viral Proteins
D000596:Amino Acids; C402641:EBNA-2 protein, Human herpesvirus 4; D019309:Epstein-Barr Virus Nuclear Antigens; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins